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Lab Skills AH
| Question | Answer |
|---|---|
| Harm caused to an individual when working in a laboratory is called a | hazard |
| Likelihood of harm arising from exposure to a hazard is termed the | risk |
| Measures to reduce risk are called | control measures |
| State two examples of hazards | Toxic/corrosive chemicals/flammable substances OR heat/pathogenic organisms/mechanical equipment |
| List two types of control measures. | 1. Appropriate handling technique 2. Protective clothing/equipment 3. Aseptic technique |
| State the form of dilution that differs by an equal interval. | Linear dilution |
| State the form of dilution that differs by a constant proportion (10 fold) dilution. | logarithmic/serial dilution 10-1, 10-2, 10-3 |
| State which type of separating technique separates substances based on density | Centrifugation |
| Explain the difference in densities between the pellet and supernatant and their location in the tube. | Pellet higher density. at bottom as solid. Supernatant liquid at top with a lower density. |
| Explain why in colorimeter a colourless solution called a blank is used before taking an absorbancy measurement. | To ensure calibration of measurement equipment for accurate results. |
| State what absorbance values of a coloured solution is an prediction of in colorimetry | Concentration of the coloured solution |
| State the effect on transmission if solution B has a higher turbidity than solution A. | Transmission reading B has a lower reading with increasing turbidity. |
| State the name for plotting measured absorbance values for known concentrations of solutions to predict the concentration of an unknown solution's concentration. | Standard curve/line |
| State the three types of chromatography. | Paper, thin layer and affinity. |
| State which two types of chromatography separate substances based on their solubility. | Paper & thin layer |
| Explain how soluble target proteins are separated from non target proteins in affinity chromatography. | only the target protein has high affinity for substances immobilised in the bead, the non target have low affinity and washed away |
| A charged macromolecules moving through a gel matrix with an n electric field applied is a description of which type of lab technique. | Gel electrophoresis |
| State one type of molecule that can be separated by gel electrophoresis. | DNA or proteins |
| State the two types of gel electrophoresis and by which property/properties they separate substances by | Native Gel Electrophoresis - size, charge and shape SDS Page—Size only - size only |
| Describe the difference in denaturing DNA between the two types of gel electrophoresis. | Native Gel electrophoresis does not denature substances. SDS page gel electrophoresis denatures substances giving them a uniform negative charge. |
| In gel electrophoresis explain how size affects the movement of proteins. | Smaller proteins move further/faster towards the POSITIVE electrode. |
| Define the term isoelectric point. | When a protein has no net charge and precipitates out of solution. |
| State the type of chemical that enables a solution to be kept at a specific pH used in isoelectric focusing. | pH buffers |
| State one example of aseptic technique. | Sterilisation by heat OR chemical means. |
| Explain why aseptic technique is necessary. | Eliminates unwanted microbial contaminants. |
| State the two types of cell culture that can be inoculated with microbes. | Agar OR broth |
| State one substance mammalian cells need in cell culture and explain why this substance is necessary. | growth factors are proteins that allow cell growth/proliferation of cells. |
| State the technique used to count viable cells. | vital staining |
| State the name of the technique used to count cells in a liquid culture via its volume. | haemocytometer |
| Explain why a liquid microbial culture is plated out on solid agar media via serial dilution and a colony count taken. | To allows the density of cells in the original culture to be estimated. |
| State the two types of microscopy and give an example of what can be viewed under each. | Bright field microscope - whole/parts of organism/dissected tissue/parts of cells. Fluorescent Microscope (higher magnification cell organelles & proteins) |
| State the term for stocks of antibodies with the same specificity. | Monoclonal antibodies |
| Give two examples of chemical labels found on antibody Immunoassays | Reporter enzymes/chemiluminescence reporters/fluorescence reporters |
| In some assay state the molecule uses to detect the presence of a specific antibody in a sample. | Antigen |
| Describe the immunoassay process. | Specific antibodies in sample bind to antigens bound to assay plate containing a chemical label. Other non specific antibodies can't bind & washed away with buffer . |
| State the name for the immunoassay used to detect a specific protein from a mixture following SDS page. | Western blotting |
| Describe what happens directly after SDS page in western blotting. | Proteins transferred/blotted onto a solid medium (nylon membrane). |
| Explain a use of immunoasssays | To determine the presence OR concentration of a particular protein. (COVID/pregnancy hormone etc.) |
Created by:
brightminds