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Biological pigments, also known as biochromes or pigments, refer to the substances or molecules that contain color because of selective color absorption. They often operate by absorbing specific wavelengths of light. As a result, the pigment color usually differs from the structural color. Whereas the pigment color is the same from all the angles, the structural color is an outcome of selective iridescence or reflection. There are usually two types of biological pigments: flower pigments and plant pigments. The color you see in flowers is because of the flower pigment. Plant pigments are responsible for controlling growth, photosynthesis, and development.

How Do Pigments in Plants Work?

Plant Pigments work by absorption of various wavelengths of light. Light is the primary source of energy and the most important environmental factor for all plants. For a plant to survive, specifically in the photosynthesis process, it needs to be absorbent to photoreceptor-treated pigments.

The measure of the wavelength of radiation that a pigment can absorb is known as the absorption spectrum. The type of pigmentation is determined by selective absorption of different wavelengths. For example, in higher plants, chlorophyll absorbs blue and red wavelengths and not green wavelengths, and this gives their leaves the green color characteristics.

The pigment’s molecular structure determines the absorption spectrum of each pigment. In this case, a pigment molecule may absorb some wavelengths and not others. This is because the molecular structure of the pigment has limited energy states that it can absorb.

Once a pigment has absorbed some wavelengths and is rejuvenated to a higher energy state, it can utilize the energy in three of the following possible ways:

  1. It can discharge it as heat.
  2. It can discharge it as radiation of a longer wavelength (lower energy).
  3. The energy can be used in photochemical work, i.e., initiation of chemical change.

Betalains, carotenoids, and Flavonoids are the common plant pigments known to emit most of their absorbed light energy as heat. Other plant pigments such as chlorophyll, rhodopsin, phycobilin, and phytochrome use much of their absorbed energy to produce various chemical changes within the plant.

It is important to note that each plant pigment reacts with a narrow range of the spectrum. Thus, there is a need to produce several other pigments with different colors to capture more sunlight energy.

Principal Pigments Explained

Plants have several pigment molecules, far more than animals. It’s because plants are creatures of light. They utilize their sense of light to manage their development, growth, and rapid response to environmental changes. Importantly, plants use light as their chief source of energy.

Plant pigments have both biological and physiological functions. For example, they can control plants’ growth, development, and photosynthesis and advertise rewards for animals that disperse seeds and pollinate flowers. There are four main types of plant pigments. Their production or retention determines their molecules, the color of leaves they fall from, and the chemical formula that describes the different atoms that make up the molecule. The four types of pigments in plants include Chlorophyll, Carotenoids, Anthocyanins, Betalains.

Chlorophyll

Chlorophyll is the green photosynthetic pigment in plants and used for photosynthesis. It is produced in the chloroplasts in the photosynthetic tissues of the leaves and occurs in algae, photosynthetic bacteria, and plants.

There are ten types of chlorophyll—chlorophyll a, b, c, d, and e, bacteriochlorophyll a, b, c, d, and e, and bacterioviridin. However, only two types of chlorophyll – chlorophyll a and chlorophyll b are more diverse in higher plants and algae. The pigment drives the process of photosynthesis, which is the process by which plants make their food. Chlorophyll reflects green light and absorbs blue and red light most strongly.

Chlorophyll is an essential pigment in plants that uses light energy to synthesize carbohydrates. All living organisms depend on photosynthesis, either directly or indirectly. Other benefits of chlorophyll include:

  • Conversion of sunlight energy into chemical energy.
  • Giving plants a green coloration.
  • Trapping sunlight, thus allowing easy and free transfer of electrons to carbon dioxide molecules.
  • Absorption of energy which then used to transform carbon dioxide and water into carbohydrates and oxygen.
  • Absorption of water and other soluble mineral salts from the soil.

The various types of chlorophyll absorb distinct wavelengths of light. The difference in absorption spectra allows a more significant portion of the solar spectrum during photosynthesis. Chlorophyll-a is common in higher plants, cyanobacteria, chloroxybacteria, and algae. Some groups of algae and higher plants also have chlorophyll-b. Several other algae groups contain chlorophyll-c and chlorophyll-d, and towards the end of the leaf’s lifespan, chlorophyll breaks down into nitrogen which the plant reabsorbs.

Carotenoids

Carotenoids are very long-chain and water-repelling plant pigments that are synthesized by many bacteria, fungi, and plants. In plants, carotenoids are in fruits, flowers, leaves, stems, and roots. Within the plant cell, carotenoids are in the plastids membrane. Chloroplasts are the most common examples of plastids that store carotenoids as well as perform photosynthesis.

Carotenoids are often red, yellow, or orange and include a familiar compound, carotene, which gives carrots their color. Beta-carotene, produced by the ray flowers’ chromoplasts, is also used in the sunflower flower plant and gives it its bright yellow-orange colors. Beta-carotene also gives other vegetables and sweet potatoes an orange color. Lycopene is another type of carotenoid pigment that gives tomatoes their red color.

The carotenoids work by absorbing the blue wavelengths and allowing the longer wavelengths to be scattered, producing the yellow color.

There are two important benefits of carotenoids in plants. Firstly, they help in photosynthesis. Carotenoid pigment helps transfer the sunlight they receive to chlorophyll, which uses it in photosynthesis. Secondly, carotenoids help in the protection of plants that are over-exposed to sunlight. This is because they dissipate excess light energy, which is absorbed as heat.

Excess light energy can destroy the protein membrane and other molecules in the absence of carotenoids. Other important functions of carotenoids include making fruits and flowers conspicuous to animals for dispersal and pollination. In addition, Beta-carotene is a good source of vitamin A in animals.

Anthocyanins

Anthocyanins are dispersed and water-soluble pigments in vacuoles, membrane-enclosed structures inside the cells that store nutrients and water. Depending on the PH, anthocyanins may appear purple, red, blue, or black. The pigments are found in fruits, flowers, and vegetables. Plants and fruits like black soybean, blueberry, black rice, raspberry, apples, roses, and wine are some of the foods rich in anthocyanins. In addition, anthocyanins are responsible for the red leaves during autumn.

Anthocyanins are synthesized through the phenylpropanoid pathway and belong to the molecule class of flavonoids. In higher plants, they often occur in fruit where they attract animals that eat fruits and disperse seeds helping in pollination. They can also be found in flowers, where they attract insect pollinators.

Although they color beverages and foods, anthocyanins have not yet been approved to be used as food additives or supplement ingredients. Some of the major benefits of anthocyanins in plants include:

Provide coloration

The blue, red, or purple coloration provided by anthocyanins can attract various herbivorous animals and insects, which may help pollination and seed dispersal plant physiology: Anthocyanins play a good role in protecting plants against extreme temperatures. For example, the tomato plant gets protection from anthocyanins against cold stress. Anthocyanins counter the reactive oxygen species minimizing the cell death in leaves.

Light absorbance

The light absorbance pattern associated with red color may help in the transfer of light to chlorophyll for purposes of photosynthesis. The red coloring may also protect leaves from herbivores that attract with the green color.

Betalains

Betalains are nitrogen-containing and water-soluble vacuolar pigments. They are characterized by red or yellow color and contain betaxanthins and betacyanins and are used as color additives in food. The pigments are often noticeable in flower petals and can also be found in leaves, fruits, roots, and stems of plants containing them. There two types of betacyanins:

  • Betacyanins: Features the reddish to violet Betalains pigments. Some of the plants that are rich in betacyanins include neobetanin, probetanin, betanin, and isobetanin.
  • Betaxanthins: Features yellow to orange Betalains pigments. Some of the common plants with betaxanthins include indicaxanthin, vulgaxanthin, portulaxanthin, and miraxanthin.
  • The key benefits of Betalains in plants include:
  • The visual attraction for seed dispersers and pollinators: The red or/and yellow color of the Betalains may attract a variety of herbivorous animals and insects, which may help in pollination and seed dispersal.
  • Provide anti-inflammatory, antioxidant, and detoxification support. Research has also shown that Betalains lessens the tumor cell growth and minimizes the risk of cancer.
  • The red or/and yellow pigments can also protect plants from herbivores attracted by the green color.

Biology Experiments to Teach this to Your Students

Modern Biology offers you exciting biological lessons geared to help you understand more about the different aspects of plant and animal life. The platform provides multi-lab programs to its students, cutting across from understanding the primary function of pigments to other complex concepts and practical experiments ranging from high school biology to molecular biology and genetics.

For questions or concerns pertaining to biological lab courses and experiments, reach out to us at (765) 446-4220 or fill out our online form today.

Just like people communicate through words, the cells that make up our bodies have a way of communicating to perform the different functions and processes that keep the body alive and responsive.

But of course, there are no talking molecules in the world of cells—they have to use cell receptors and signaling sequences to pass information from one cellular region to another. This is achieved through receptors (receiving molecules) and ligands (signaling molecules). 

Receptors and ligands come in various forms, but they always have one trait: they come in pairs, with a receptor recognizing just one (or a few) particular ligands and a ligand attaching to only one (or a few) target receptors. When a ligand binds to a receptor, it alters its shape or function, enabling it to send a signal or cause a change within the cell.

One important component that allows this type of signaling is the cell surface receptor. Let’s look at what exactly cell surface receptors are and their role in converting information from outside the cell into a change within the cell.

In a nutshell, cell surface receptors also known as transmembrane receptors are membrane-linked proteins that bind to ligands (signaling molecules) outside the cell surface and perform signal transduction by converting extracellular signals into intracellular signals.

The ligand doesn’t have to penetrate the plasma membrane in this kind of signaling. As a result, ligands may be a wide range of molecules from large to hydrophilic (water-loving) compounds. A typical cell-surface receptor contains three domains or protein regions: 

  • An extracellular domain (outside the cell) ligand-binding domain,
  • A hydrophobic domain that extends through the membrane
  • An intracellular domain (inside the cell) which often sends a signal.

Signal Transduction

A series of biochemical changes that occur inside the cell or the alteration of the cell membrane potential by the flow of ions in and out of the cell sustain signal transmission. Receptors that cause biochemical changes may either directly or indirectly activate intracellular messenger molecules via intrinsic enzymatic activity inside the receptor. The transduction process requires four parts:

  • Extracellular signaling molecule: Produced at one cell but can move from cell to cell
  • Intracellular signaling proteins: Transmit the signal to the cell components
  • Target proteins: Altered when an active signaling pathway and changes the behaviors of a cell
  • Receptor protein: Bind to the signaling molecule and help pass information into the cell

The activation and/or inhibition of signaling cascades that control various cellular activities, such as cell growth, proliferation, survival, and invasion, are triggered by ligand binding and cell surface and internal receptors’ activation. The diagram below represents a signal transduction pathway.

The Three Types of Cell Surface Receptors

The hydrophobic region may consist of several stretches of amino acids that crisscross the membrane, and the size and structure of these sections may vary greatly depending on the kind of receptor. There are many kinds of cell surface receptors, but at this time, we’ll look at the three primary receptors: Ion channel-linked receptors, G protein-linked receptors, and Enzyme-linked receptors. 

Ion Channel-Linked Receptor

The neurotransmitter binds to the receptor and changes the protein structure during signal transduction in a neuron. This allows extracellular ions to enter the cell by opening the ion channel. As a result, the plasma membrane’s ion permeability is altered, converting the extracellular chemical signal into an intracellular electric signal that affects cell excitability.

The acetylcholine receptor is a cation channel-linked receptor. There are four subunits in the protein: alpha (α), beta (β), gamma (γ), and delta (δ). There are two alpha (α) subunits, each of which has an acetylcholine binding site. Moreover, there are three possible conformations for this receptor. The native protein conformation is closed and unoccupied. 

When two acetylcholine molecules attach to the binding sites on alpha (α) subunits, the receptor’s conformation is changed, and the gate is opened, enabling numerous ions and tiny molecules to pass through. However, this open and occupied state only lasts a short time after which the gate is closed, resulting in the closed and occupied state. In this case, the two acetylcholine molecules dissociate from the receptor, restoring it to its original closed and unoccupied condition.

G-Protein-Linked Receptors

The G-protein is a trimeric protein made up of three subunits designated as alpha (α), beta (β), gamma (γ). The alpha (α) subunit releases bound guanosine diphosphate (GDP) in response to receptor activation, which is then displaced by guanosine triphosphate (GTP), resulting in the activating the subunit, which subsequently dissociates from the β, and γ subunits, and the cycle starts all over again. The activated subunit may also have a direct effect on intracellular signaling proteins or target functional proteins.

In eukaryotes, G-protein-linked receptors (GPCRs) are the most numerous and varied category of membrane receptors. Light energy, peptides, lipids, carbohydrates, and proteins all pass via these cell surface receptors, which serve as an inbox for communications. Cells receive these signals to notify them of the presence or absence of life-sustaining light or nutrients in their surroundings or to relay information from other cells.

GPCRs are involved in a wide range of activities in the human body, and a better knowledge of these receptors has had a significant impact on contemporary medicine. In fact, experts believe that GPCRs are involved in the action of one-third to half of all marketed drugs.

Photosensitive chemicals, odors, pheromones, hormones, and neurotransmitters are examples of ligands that bind and activate the G-protein-linked receptors, and they vary in size from small molecules to peptides and large proteins. The cAMP signaling pathway and the phosphatidylinositol signaling pathway are the two main transduction pathways involving G-protein coupled receptors. Both are mediated by the activation of G proteins.

Enzyme-Linked Receptors

Enzyme-Linked Receptors (mainly receptor tyrosine kinases) are Cell-surface receptors with intracellular domains connected to an enzyme. In certain instances, the receptor’s intracellular domain is an enzyme, and in some, the enzyme-linked receptor’s intracellular domain interacts directly with an enzyme. Examples of enzyme-linked receptors include: 

  • Receptor tyrosine kinases (RTKs), 
  • Receptor serine/threonine kinases, 
  • Receptor-like tyrosine phosphatases, 
  • Histidine kinase-associated receptors, and 
  • Receptor guanylyl cyclases

Receptor tyrosine kinases are the most common and have the most applications. Growth factors such as epidermal growth factor (EGF), platelet-derived growth factor (PDGF), fibroblast growth factor (FGF), hepatocyte growth factor (HGF), nerve growth factor (NGF), and hormones such as insulin bind to the majority of these molecules.

After binding with their ligands, most of these receptors will dimerize in order to trigger further signal transductions. When the epidermal growth factor (EGF) receptor binds to its ligand EGF, the two receptors dimerize, and the tyrosine residues in the enzyme part of each receptor molecule are phosphorylated. This activates the tyrosine kinase, which then catalyzes further intracellular processes.

Receptor tyrosine kinases can be broken up into seven categories. Each subgroup is represented by just one or two members. In certain subfamilies, the tyrosine kinase domain is interrupted by a “kinase insert region.” The functions of the majority of cysteine-rich, immunoglobulin-like, and fibronectin-type III-like domains are not yet known.

Phosphate groups are removed from phosphotyrosine residues by receptor-tyrosine phosphatases, which counteract the actions of receptor-tyrosine kinases. Receptor tyrosine phosphatases, in many instances, act as negative regulators in cell signaling pathways, ending signals started by protein-tyrosine phosphorylation. On the other hand, some protein-tyrosine phosphatases are cell surface receptors whose enzymatic activities aid cell signaling. 

A receptor called CD45, which is expressed on the surface of T and B cells, is an excellent example. CD45 is believed to dephosphorylate a particular phosphotyrosine after antigen stimulation, inhibiting the enzymatic activity of Src family members. As a result, the CD45 receptor-tyrosine phosphatase stimulates nonreceptor protein-tyrosine kinases, which is rather paradoxical.

The extracellular and intracellular domains of enzyme-linked receptors are typically extensive, but the membrane-spanning portion is made up of one alpha-helical peptide strand. When a ligand attaches to the extracellular domain, a signal is sent across the membrane, activating the enzyme, which puts in motion a series of processes inside the cell that ultimately results in a cellular response.

Cell disorders such as cancer are defined by anomalies in cell growth, proliferation, differentiation, survival, migration, and anomalies in signaling through enzyme-linked receptors. This is evidence that Enzyme-linked receptors play a significant role in the development of this class of illnesses. 

There are many lab experiments that can be conducted to observe the cell surface structure and help you familiarize yourself with the current strategies used in the study of cell surface receptors and other important regulatory molecules. At Modern Biology Inc, we have high-quality educational products and experiments to help students and tutors when learning about cell surface receptors and other important biological concepts. For more information, reach out to us at (765) 446-4220 or fill out our online form, and one of our team members will get back to you in a jiffy.

The polymerase chain reaction, more commonly referred to as PCR, is sometimes explained as “molecular photocopying.” PCR is an inexpensive and convenient way to copy or “amplify” small chains of DNA into samples larger enough for molecular and genetic analyses.

PCR uses relatively short DNA sequences known as primers to choose the portion of the genome to be amplified. The sample is buffered in a saline solution to keep pH constant, and DNA-replicating enzymes are added. The temperature of the mixture is raised and lowered repeatedly over a period of several hours to assist a DNA replication enzyme in copying the primer. The result is up to a billion copies of the prime DNA sequence in just a few hours.

Once a strand of DNA has been amplified by PCR, the product can be used in a variety of laboratory procedures. PCR is a first step in testing for many kinds of bacteria and viruses, including HIV and COVID-19. Amplified DNA is useful in the detection of many genetic disorders. And the human genome project would not have been possible without PCR.

Prior attempts to decode the human genome had relied on techniques that would begin at one telomere of a strand of DNA and attempt to read millions of bases until it reached the telomere at the other end. With PCR, however, the human genome project sequenced multiple strands of DNA at different places but at the same time. The cost of reading the human genome was reduced by a factor of over 100,000 and sped up by years.

There are a huge number of applications of PCR beyond the human genome project. PCR might be used by a researcher who wants to study a single gene. Or maybe a crime scene detective is looking for a genetic marker to rule out a suspect or justify further investigation. Or an ancestry service may want to match DNA sequences between people who don’t know each other to confirm that they are biologically related.

PCR is widely regarded as one of the most important advances in the study of molecular biology in the twentieth century. Its creator, Kary B. Mullis, was awarded the Nobel Prize for Chemistry in 1993.

PCR Process Steps Explained

The three PCR steps seem almost intuitive since the technique has been so widely used, although the invention of PCR was revolutionary in its time. Before the steps make sense, however, there are two inputs into PCR testing about which we need to give further detail.

Taq Polymerase

Cells have to replicate their DNA with a DNA polymerase before they can divide. The DNA polymerases that power mitosis make new strands of DNA on existing strands of DNA they use as templates.

PCR uses a specialized polymerase known as the Taq polymerase. This polymerase gets its name from the thermophilic bacterium in which it was first isolated, Thermus aquaticus. This bacterium lives in thermal vents of underwater volcanoes. It survives at temperatures that would denature proteins and enzymes in most other species. Its polymerase is optimally active at temperatures around 70° C, or 158° F for your students.

Heat stability is what makes the Taq polymerase the ideal choice for PCR. This procedure makes repeated use of high temperatures to denature and separate the strands of DNA as they are replicated.

PCR Primers

Polymerases, including Taq polymerase, can only make DNA if they are given a template, the primer we mentioned previously. Every polymerase uses a short sequence of A-C-G-T nucleotides as a starting point. The experimenter chooses the primers that will be amplified by the Taq polymerase in PCR.

Primers are very short chains of DNA, usually around just 20 nucleotides long. Every PCR reaction uses two primers chosen to flank the target region to be copied. This way the primer bind to opposite strands of DNA, at both edges of the segment the experimenter seeks to copy. The primers then bind to the DNA template by pairing complementary bases. An A-G-C-T-A-G-C-T-A-G-C-T-A-G-C-T template would bond to a T-C-G-A-T-C-G-A-T-C-G-A-T-C-G-A primer.

Once the primers bind to the template, they are extended by the Taq polymerase, and the nucleotides between them will be copied.

Those basics out of the way, we can now talk about the 3 steps of PCR.

3 Steps of PCR

The essentials of PCR are the Taq polymerase, template DA, primers, and the A-G-C-T nucleotides. The experimenter assembles these ingredients in a tube, along with the cofactors that regulate the kinetics of the Taq enzyme, and puts the mixture through repeated heating and cooling that power the synthesis of DNA.
The three basic steps are:

  1. Denaturation at 96° C, heating the polymerase, DNA to be copied, primers, and nucleotides so strongly that the sample DNA is denatured. Its strands unravel. Denaturation converts double-stranded DNA to single-stranded DNA for the next step.
  2. Annealing at 55 to 65° C cools the reaction, so the priers can bind to their complementary nucleotide sequences
  3. Extension at 72° C raises the reaction temperature so Taq is active, extending the primers, and synthesizing new strands of DNA.

PCR repeats this cycle 25 to 35 times over a typical reaction that takes two to four hours. Copying shorter segments of DNA takes less time, and copying longer segments of DNA takes more time. Efficient PCR reactions can create billions of copies of DNA, because it’s not just the original DNA that is used as a template each time. Every copy of DNA serves as a template for the next round of synthesis.

The number of DNA molecules roughly doubles with each reaction. As a result, 25 rounds of PCR can create 2 25 or over 30 million copies of the DNA being studied, and 35 rounds of PCR can create 235 or over 34 billion copies of the target DNA.

Visualizing PCR Results with Gel Electrophoresis

The next step in characterizing DNA (usually) is visualizing the results of PCR with gel electrophoresis. As students of teachers who use Modern Biology’s gel electrophoresis supplies and all-in-one gel electrophoresis laboratory teaching kits are well aware, gel electrophoresis is a technique that uses electrostatic charge to pull segments of DNA through a gel matrix. DNA is dyed with ethidium bromide, so it glows under UV light. Experimental and control samples of DNA are placed at one end of a buffered gel (buffered with saline to keep pH stable) in wells covered by the conductive gel.

DNA has a slight negative charge, so DNA samples are placed nearest the cathode, the negative charge attached to the gel. They are pulled toward the anode, the positive charge at the other side of the gel. Shorter segments get pulled faster than longer segments, so when DNA is visible at the anode side of the gel, power is turned off.

If everything has gone as planned, the electrostatic charge has created a “ladder” of DNA samples with known base pair lengths at one side of the gel, and the tested DNA has arrived near or between two controls that give a rough estimate of how many base pairs are in the sample. The length of the DNA in the sample is now estimated, and the millions or billions of copies of test DNA now visible under UV light, can be cut out of the gel for further analysis.

Practical Applications of PCR

One of the questions that comes up in biology classes at all levels since the beginning of the pandemic is “What is a COVID-19 test, anyway?” The answer is, although there are several approaches to COVID-19 detection, the most commonly used method is a highly automated polymerase chain reaction test.

Real-time PCR amplifies a known primer of COVID-19 DNA that does not carry the risk of causing disease. Amplifying this segment of DNA tens of millions of times, that is, if it is to be found on the swab, automated detection equipment can detect COVID-19 with 97-percent specificity and 100-percent sensitivity. Chances are that many of your students will have had PCR testing.

PCR, of course, has many other applications that pique student interest. PCR can be used to amplify fetal DNA from a tiny sample of amniotic fluid to test for genetic issues. PCR can amplify bacterial or viral DNA to test for the presence of pathogens in a patient’s bone sample, skin sample, serum, or spinal fluid.

PCR is of enormous value in forensics. The DNA in a single hair follicle can be amplified for testing that can exclude an innocent suspect or point to the need for further investigation to establish probable cause for an arrest.

Modern Biology provides everything busy biology instructors need to introduce their students to hands-on experiences of PCR. Our experiments aren’t just demonstrations of PCR. Your students will use PCR to confirm or disconfirm a scientific hypothesis of their own making. And if you want to go beyond our experiments, we have all the PCR supplies you need.

Modern Biology supports experiential learning through biology experiments for over 500,000 students. Let us show you why over 80,000 teachers trust Modern Biology.

Hands-on ELISA testing is a great way to make molecular biology relevant to your students.


Two of the biggest epidemics in the last 40 years, epidemics all of your students will know about, have been the human immunodeficiency virus that causes AIDS, and the SARS-CoVirus 2, more commonly known as COVID-19. The ELISA amino acid assay has proven just as useful for testing for COVID-19 as it was in testing for HIV 40 years ago.

Your students may also be interested in knowing that ELISA has been adapted for home pregnancy tests. In the clinic, it’s used to test for prostate cancer and the antibodies generated in lupus, rheumatoid arthritis, and other autoimmune diseases they will encounter further in their studies.
Students will know what ELISA is used for, even if they couldn’t explain what the technique is, as in this sample answer for the study question, “What is ELISA?”


ELISA is a powerful method for detecting specific proteins in complex protein mixtures. It continues to be used more and more in medicine to detect antibodies produced in response to the presence of pathogens like those produced by HIV and the novel coronavirus. Just in the last few months of 2020, advances in ELISA testing have made a “spit test” for COVID-19 possible. A commercially available, serum-based enzyme-linked immunosorbent assay has made rapid testing for the virus possible with 100% specificity, in much the same vein as rapid ELISA tests for HIV that have been around for several years.
Teachers can motivate their students to pay attention with ELISA. And the steps for carrying out Modern Biology’s IND-03: ELISA immunoassay couldn’t be easier. In this experiment, students use a tried-and-true procedure to bind an antigen to the walls of the microplate, bind an enzyme-linked antibody to the antigen, and then use that enzyme to detect the presence of the antigen, indicating infection. 
Polymerase Chain Reaction (PCR) testing has also been used as a detection method for COVID. Amplification of viral RNA makes it much easier to see the small quantities of DNA required for testing. Both PCR and ELISA are rapid tests your students can accomplish quickly, within a typical lab period. Later in your course, your students can work with the lab materials supplied by IND-07: Amplification of a Hemoglobin Gene by PCR to amplify a few nanograms of DNA into a few milligrams of DNA in just a few hours, and then IIND-21: Identifying Genomic and Plasmid DNA Sequences in E. coli by Colony PCR to amplify specific DNA sequences without DNA purification.

Polymerase-chain-reaction


Steps for This Experiment
It is useful to explain to students that direct ELISA in medical labs is typically performed in a 96-well microtiter plate by a chemical reaction that results in the covalent attachment of antigen, which is most often a protein, through its free amino groups. The test then involves probing each coated well with an antibody specific for the target antigen, probing that bound antibody with a second antibody specific for the stable region of the first antibody, and using a variety of detection methods. Different enzymes result in different color changes that can be read automatically with a scanner in some lab settings, or in the case of this experiment, can be seen with the naked eye.
What’s involved in teaching these labs? Let’s consider the easy steps for teaching Modern Biology’s IND-03: ELISA immunoassay.

  1. In this lab, your students will be using a goat-anti-rabbit IgG antibody to study the specificity of an antibody antigen reaction, in order to compare the binding of this antibody serum to IgGs in serum from chicken, cow, horse, and rabbit. To aid in this, the anti-rabbit IgG has been covalently linked to peroxidase, which will catalyze a color producing reaction, so that your students can study the results without the aid of specialized equipment.
  2. Assign your students to work in pairs. The ELISA Immunoassay kit will include the reagents and testing materials necessary for the experiment to be performed twice by 8 groups, or once by 16 groups of students. Make sure that each group has read the guide included with your supplies before commencing the lab, and have all of the included materials, as outlined in the experiment guide.
  3. Your student groups will need to number the provided microtitration plate. These plates usually come in a size to accommodate 96 wells over their surface, but for the purposes of this experiment, they will be provided with a 1/4 section of a standard plate, resulting in a plate that contains 24 wells. These plates should be labeled so that across the top of the grid reads the numbers one through six, and down the left-hand side are the letters A to D for clear tracking of the experiments.
  4. Next, they will need to proceed with the absorption of the antigen, which will require the students to perform serial, ten-fold dilutions of the sera, after which the plate will need be left undisturbed for twenty minutes to provide adequate time for the proteins to be adsorbed to the well surfaces. Afterwards, your students will use TBS-gelatin to block sites on the plastic that are not bound to serum proteins. Once this process is complete, they will use pipettes to carefully discard the liquids in each well, preparing them for the antibody reaction.
  5. From here, your students will add the goat anti-rabbit IgG peroxidase to each well and rotate the plate to ensure that all surfaces at the bottom of each well comes into appropriate contact with the anti-body solution. The plate will again need to be left alone for 20 minutes, so that the antibody can properly bind to the immobilized IgG. After this, TBS-gelatin will again be utilized, and the excess solution discarded as done previously.
  6. The final step for your students will be to use the provided color development solution in each well, and then wait 15 minutes for change to occur. After this, the microtitration plate can be placed over a blank piece of white paper so that the intensity of the blue and yellow product can be examined and compared.
    Get All the Experiment Supplies and Equipment You need for Your Students
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Biology survey courses in college sometimes turn on students to new careers in the health and life sciences. And survey courses in biology in college never have to be dull. Modern Biology Inc. produces complete kits — reagents, test materials, and teaching guides — every intro biology instructor can use to keep college students engaged.
Here are four examples of cool and engaging experiments:

1. Gel Electrophoresis
Many introductory biology students have not learned the concept of what proteins are, or how they might be observed and compared, until they participate in a lab exercise like our EXP-101 Electrophoretic Separation of Proteins. In this experiment, students are not just watching a demonstration of how scientists identify proteins. They will have a hands-on experience with electrophoresis in the lab in which they can compare the migration of a control against the migration of an experimental protein across a charged agarose gel.

2. Sickle Cell Anemia
Just about all college biology students will have some knowledge of sickle cell disease. Most just haven’t dug deeper into learning about heterozygous sickle cell trait, or how it’s possible to test for the genes that cause it — until they do actual blood testing for sickle cell genes in our EXP 102: Genetics and Sickle Cell Anemia. In this experiment, students will first study the differences in electrophoretic dispersal of normal hemoglobin and hemoglobin from a person who has sickle cell trait. Then they can *optionally* test their own blood for sickle cell genes.

hbss - sickle cell

3. Cell Respiration
There’s more to experimental biology than electrophoresis, of course. In B4-1: Effects of Temperature on Cell Respiration, your students will first rethink their understanding of how animals breathe in oxygen and breathe out carbon dioxide, but plants must somehow be oxygen producers 24/7. In this experiment, your students will measure oxygen consumption and hydrogen liberation of germinating seedlings with respirometers at varying temperature levels. They will use dyes to create a visual, analog measurement of respiration in plants for graphic confirmation or disconfirmation of their hypotheses about the nature of plant respiration in seedlings.

4. Cell Surface Receptors
In EXP 702: Analysis of a Cell Surface Receptor, your students will learn about their own cell surface receptors from a buccal swab. They will study multiple sites for concanavalin A binding and the hemagglutination reaction in their own cells.

Great Experiments and Supplies for Your Students

Modern Biology’s products are always fully engaged experiments, never demonstrations. Our reagents and test solutions are the real deal.

Modern Biology ensures that our products are non-toxic and safe for student use. Student safety is paramount in every product we create.

Modern Biology takes the hassle out of sourcing reagents and test materials. Our experiments are complete with reagents, disposable labware and digital instructions. Modern Biology has tailored our experiments so that the same equipment can be used with either our Protein or DNA labs.

Modern Biology empowers you to integrate the scientific method into what can often become a descriptive course. We take care of your ordering and inventory tasks for over 20 hours of laboratory instruction, while pricing our products to fit public school budgets.

Over 500,000 students have learned biology with the help of Modern Biology products. We want to show you why thousands of teachers trust Modern Biology.