| Journal Articles: 19 results |
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Glycosyltransferases A and B: Four Critical Amino Acids Determine Blood Type Natisha L. Rose, Monica M. Palcic, and Stephen V. Evans
Human A, B, and O blood type is determined by the presence or absence of distinct carbohydrate structures on red blood cells. In this review the chemistry of the blood group ABO system and the role of glycosyltransferase A, glycosyltransferase B, and the four amino acids critical to determining blood group status are discussed.
Rose, Natisha L.; Palcic, Monica M.; Evans, Stephen V. J. Chem. Educ. 2005, 82, 1846.
Carbohydrates |
Enzymes |
Kinetics |
Bioorganic Chemistry |
Crystals / Crystallography |
Molecular Biology |
X-ray Crystallography |
Amino Acids
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Removal of Zinc from Carbonic Anhydrase. A Kinetics Experiment for Upper-Level Chemistry Laboratories Kathryn R. Williams and Bhavin Adhyaru
The Zn(II) ion in the active site of carbonic anhydrase can be removed by complexation with 2,6-pyridinedicarboxylate (dipicolinate).
Williams, Kathryn R.; Adhyaru, Bhavin. J. Chem. Educ. 2004, 81, 1045.
Kinetics |
Biophysical Chemistry |
Nuclear / Radiochemistry |
Enzymes |
Instrumental Methods
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Collaboration between Chemistry and Biology to Introduce Spectroscopy, Electrophoresis, and Molecular Biology as Tools for Biochemistry Vicky L. H. Bevilacqua, Jennifer L. Powers, Connie Tran, Swapan S. Jain, Reem Chabayta, Dale L. Vogelien, Ralph J. Rascati, Michelle Hall, and Kathleen Diehl
Program that integrates a variety of instrumental techniques across the biological and chemistry curricula, including biochemistry, plant physiology, genetics, and forensics.
Bevilacqua, Vicky L. H.; Powers, Jennifer L.; Vogelien, Dale L.; Rascati, Ralph J.; Hall, Michelle; Diehl, Kathleen; Tran, Connie; Jain, Swapan S.; Chabayta, Reem . J. Chem. Educ. 2002, 79, 1311.
Biotechnology |
Enzymes |
Forensic Chemistry |
Hormones |
Instrumental Methods |
Kinetics |
Plant Chemistry |
Proteins / Peptides |
UV-Vis Spectroscopy
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Factors Affecting Reaction Kinetics of Glucose Oxidase Kristin A. Johnson
Demonstration based on a biochemical kinetics experiment in which the rate of reaction varies with the enzyme concentration, substrate concentration, substrate used in the reaction, and temperature.
Johnson, Kristin A. J. Chem. Educ. 2002, 79, 74.
Enzymes |
Kinetics |
Proteins / Peptides |
Carbohydrates |
Catalysis |
Rate Law
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A Simple Method for Demonstrating Enzyme Kinetics Using Catalase from Beef Liver Extract Kristin A. Johnson
A simple visual method of demonstrating enzyme kinetics using beef liver catalase. Filter paper is saturated with beef liver extract and placed into a solution of hydrogen peroxide. The catalase in the extract decomposes the hydrogen peroxide to water and oxygen. Oxygen forms on the filter paper, and the filter paper rises to the top of the beaker. Catalase activity is measured by timing the rise of the enzyme-soaked filter paper to the top of beakers containing different concentrations of hydrogen peroxide.
Johnson, A. Kristin. J. Chem. Educ. 2000, 77, 1451.
Enzymes |
Kinetics |
Proteins / Peptides |
Reactions
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Enzymatic Spectrophotometric Reaction Rate Determination of Glucose in Fruit Drinks and Carbonated Beverages. An Analytical Chemistry Laboratory Experiment for Food Science-Oriented Students Argyro-Maria G. Vasilarou and Constantinos A. Georgiou
This laboratory experiment demonstrates the implementation of reaction rate kinetic methods of analysis, the use of enzymes as selective analytical reagents for the determination of substrates, the kinetic masking of ascorbic acid interference, and the analysis of glucose in drinks and beverages.
Vasilarou, Argyro-Maria G.; Georgiou, Constantinos A. J. Chem. Educ. 2000, 77, 1327.
Enzymes |
Food Science |
Kinetics |
Quantitative Analysis |
Carbohydrates
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Kinetics of Papain: An Introductory Biochemistry Laboratory Experiment Kathleen Cornely, Eric Crespo, Michael Earley, Rachel Kloter, Aime Levesque, and Mary Pickering
In this experiment, we investigate the kinetics of the thiol protease papain. A specific substrate, Na-benzoyl-arginine-p-nitroanilide (BAPNA), is used, which takes advantage of the fact that papain interacts with a phenylalanine residue two amino acids away from the peptide bond cleaved. Upon hydrolysis by papain, a bright yellow product is released, p-nitroaniline. This allows the reaction to be monitored spectrophotometrically by measuring the rate of formation of the p-nitroaniline product as a function of the increase in absorbance of the solution at the lmax of p-nitroaniline (400 nm) over time at various substrate concentrations. These data are used to plot a Lineweaver-Burk plot from which the vmax and KM are obtained.
Cornely, Kathleen; Crespo, Eric; Earley, Michael; Kloter, Rachel; Levesque, Aime; Pickering, Mary. J. Chem. Educ. 1999, 76, 644.
Enzymes |
Kinetics |
UV-Vis Spectroscopy
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A Simple Method To Demonstrate the Enzymatic Production of Hydrogen from Sugar Natalie Hershlag, Ian Hurley, and Jonathan Woodward
In the experimental protocol described here, it has been demonstrated that the common sugar glucose can be used to produce hydrogen using two enzymes, glucose dehydrogenase and hydrogenase. No sophisticated or expensive hydrogen detection equipment is required-only a redox dye, benzyl viologen, which turns purple when it is reduced. The color can be detected by a simple colorimeter.
Hershlag, Natalie; Hurley, Ian; Woodward, Jonathan. J. Chem. Educ. 1998, 75, 1270.
Enzymes |
Kinetics |
UV-Vis Spectroscopy |
Carbohydrates |
Applications of Chemistry
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Disadvantages of Double Reciprocal Plots R. Bruce Martin
Because they involve grossly uneven weightings of points, the linear and formally similar double reciprocal Benesi-Hildebrand and Lineweaver-Burke plots should never be used to resolve equilibrium and enzyme kinetic results.
Martin, R. Bruce. J. Chem. Educ. 1997, 74, 1238.
Biophysical Chemistry |
Enzymes |
Equilibrium |
Kinetics
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The Well-Read Biochemist Gale Rhodes
This article describes how I use a collection of poems, essays, and fiction to inspire my biochemistry students to make connections between the arcane world of cellular chemistry and the wider world of literature and the humanities.
Rhodes, Gale. J. Chem. Educ. 1996, 73, 732.
Enzymes |
Kinetics |
Metabolism |
Proteins / Peptides |
Membranes
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Breaking Bonds versus Chopping Heads: The Enzyme as Butcher Todd P. Silverstein
Analogy to help biochemistry students understand concepts of Michaelis-Menten kinetics; active site/binding site; activation energy; substrate saturation; cooperativity; allosteric effects; and inhibitors.
Silverstein, Todd P. J. Chem. Educ. 1995, 72, 645.
Catalysis |
Enzymes |
Kinetics |
Proteins / Peptides |
Mechanisms of Reactions |
Reactions |
Rate Law
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On the Use of Least Squares To Fit Data in Linear Form Chong, Delano P.
Analysis of Michaelis-Menten kinetics as an example of using least squares to fit data in a linear form.
Chong, Delano P. J. Chem. Educ. 1994, 71, 489.
Chemometrics |
Enzymes |
Kinetics
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A biochemistry project to study mushroom tyrosinase: Enzyme localization, isoenzymes, and detergent activation Rodriquez, Marta Olga; Flurkey, William H.
Investigating mushroom tyrosinase isoenzymes in different tissue sections of commercial mushrooms.
Rodriquez, Marta Olga; Flurkey, William H. J. Chem. Educ. 1992, 69, 767.
Enzymes |
Electrophoresis |
Kinetics
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Effects of "crowding" in protein solutions Ralston, G. B.
The effects of macromolecular nonideality and crowding on chemical equilibria, association reactions, and enzyme kinetics.
Ralston, G. B. J. Chem. Educ. 1990, 67, 857.
Proteins / Peptides |
Equilibrium |
Reactions |
Enzymes |
Kinetics
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Analysis of kinetic data with a spreadsheet program Henderson, John
An article about spreadsheet templates that accept concentration versus time data for several runs of an experiment, determination of least-squares lines through data points for each run, and will allow the user to exclude points from the least-squares calculation.
Henderson, John J. Chem. Educ. 1988, 65, A150.
Chemometrics |
Laboratory Computing / Interfacing |
UV-Vis Spectroscopy |
Rate Law |
Kinetics |
Enzymes
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Cycloamyloses Bergeron, Raymond J.
Examines an unusual carbohydrate system of current interest in the hope of generating some enthusiasm for the topic.
Bergeron, Raymond J. J. Chem. Educ. 1977, 54, 204.
Carbohydrates |
Molecular Properties / Structure |
Thermodynamics |
Kinetics |
Enzymes |
Spectroscopy
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The principle of exponential change: Applications in chemistry, biochemistry, and radioactivity Green, Frank O.
Examines the nature of exponential change and its applications to chemistry, biochemistry, and radioactivity, including radioactive decay, enzyme kinetics, colorimetry, spectrophotometry, and first order reaction kinetics.
Green, Frank O. J. Chem. Educ. 1969, 46, 451.
Nuclear / Radiochemistry |
Kinetics |
Enzymes |
Spectroscopy
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Reaction rate analysis and instrumentation: An experiment for the analytical laboratory Pardue, Harry L.; Burke, Michael F.; Jones, David O.
This experiment exemplifies the use of operational amplifiers for measurement and analog computation in determining the glucose utilizing glucose enzyme.
Pardue, Harry L.; Burke, Michael F.; Jones, David O. J. Chem. Educ. 1967, 44, 684.
Kinetics |
Rate Law |
Catalysis |
Enzymes |
Carbohydrates
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Determination of glucose: A kinetics experiment for the analytical course Toren, E. Clifford, Jr.
This determination of glucose demonstrates both kinetic and enzymatic methods of analysis.
Toren, E. Clifford, Jr. J. Chem. Educ. 1967, 44, 172.
Quantitative Analysis |
Carbohydrates |
Kinetics |
Enzymes
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