On the nature of p-nitrothiophenylated myosin
| Autor: | Robert G. Wolcott, Paul D. Boyer |
|---|---|
| Rok vydání: | 1973 |
| Předmět: |
Binding Sites
Stereochemistry Disulfide Linkage Chemistry Chromatography Paper macromolecular substances Borohydrides Myosins Sulfides Tritium Biochemistry Genetics and Molecular Biology (miscellaneous) Nitrophenols chemistry.chemical_compound Adenosine Triphosphate Biochemistry Myosin Chromatography Gel Animals Magnesium Disulfides Rabbits Amino Acids Derivative (chemistry) Protein Binding |
| Zdroj: | Biochimica et biophysica acta. 303(2) |
| ISSN: | 0006-3002 |
| Popis: | Evidence is presented that myosin exposed to p-nitrothiophenol, ATP, and Mg2+ near o °C does not form a thiolester derivative as has been reported (Kinoshita, N., Kubo, S., Onishi, H. and Tonomura, Y. (1969) J. Biochem. Tokyo 65, 285–301). Properties of the p-nitrothiophenylated myosin and of model p-nitrothiophenyl esters suggest that the p-nitrothiophenol is bound to the myosin by a disulfide linkage. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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