| Autor: |
Biellmann, Jean-François, Goulas, Philippe R., Nicolas, Jean-Claude, Descomps, Bernard, Crastes de Paulet, André |
| Předmět: |
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| Zdroj: |
European Journal of Biochemistry; 8/15/79, Vol. 99 Issue 1, p81-84, 4p |
| Abstrakt: |
3-Chloroacetylpyridine-adenine dinucleotide phosphate is both active as a hydride acceptor and inactivates estradiol 17β-dehydrogenase. This coenzyme analogue behaves like an affinity label. The inactivation kinetics are discussed in relation to those observed with 3-chloroacetylpyridine- adenine dinucleotide. The pH dependence of the rate of inactivation, in combination with determination of the number of reactive cysteine residues, pointed to the alkylation of one cysteine residue/subunit. The stoichiometry was one molecule of dinucleotide per subunit and no cooperativity was detected. When 14C-labeled dinucleotide was used, the 14C label was found mainly in one peptide, accounting for 90% of the incorporated radioactivity, whereas in previous work it had been shown that 3-chloroacetylpyridine-adenine dinucleotide is an affinity reagent which labels three peptides. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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