Laboratory Guide to Biochemistry, Enzymology and Protein Physical Chemistry: A Study of Aspartate Transcarbamylase. This item is unavailable.
Language: English
Published by Springer, 1991
- Hardcover
- New

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- Title
- Laboratory Guide to Biochemistry, Enzymology and Protein Physical Chemistry: A Study of Aspartate Transcarbamylase
- Author
- Marc Le Maire Raymond Chabaud Guy Herve
- Publisher
- Springer
- Publication year
- 1991
- Condition
- New
- Binding
- Hardcover
- Language
- English
- ISBN 10
- 0306436396
- ISBN 13
- 9780306436390
1 Aspartate Transcarbamylase.- 2 Molecular Genetics: Regulation of Aspartate Transcarbamylase Biosynthesis.- 3 Purification of Aspartate Transcarbamylase and Its Subunits.- 4 Structural and Physicochemical Study of Aspartate Transcarbamylase.- 5 Enzymatic Catalysis and Regulation.- 6 Complementary Experiments.- 1. Equations and Units.- 2. Molar Mass and Molecular Mass.- 3. Units of Catalytic Activity.- 4. Units of Radioactivity.- 5. Units of Quantity.- 7. Calculation of Acceleration.- 8. Bacterial Strains.- 9. Solutions and Reagents.- 9.1. 0.8-M Tris-Acetate Buffer, pH 8.- 9.2. 0.2-M Acetic Acid.- 9.6. Elution Buffer for Chromatography: 10 × Stock Solution.- 9.7. 100-mM Aspartate, pH 8.- 9.8. 10-mM Carbamylaspartate, pH 8.- 9.9. 1-M Phosphate Buffer, pH 7.2.- 9.10. Buffer for Dilution of E.- 9.11. Buffer for Dilution of C.- 9.12. Buffer for Dilution of R and Recombination.- 9.13. 200-mM Cacodylate Buffer, pH 6, 7, and 7.5.- 9.14. 200-mM Tris-Acetate Buffer, pH 8 and 9.- 9.15. 200-mM Glycine Buffer, pH 10.- 9.16. 400-mM Succinate, pH 7.- 9.17. Reaction Medium: 20-mM CAP-200-mM Tris-Acetate, pH 8.- 10. Preparation of Standard Protein Mixtures for Column Calibration.- Answers To Questions.- References.
"Synopsis" may belong to another edition of this title.
Synopsis
This guide for a laboratory course presents an integrated set of experiments relying entirely on the use of unique enzyme, aspartate transcarbamylase, which exhibits all of the catalytic and regulatory properties characteristic of allosteric enzymes. A comprehensive study of this enzyme and its dissociated subunits leads to the use of numerous bioc
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