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English1. Adenosine deaminase was inactivated by 9-(4-bromoacetamidobenzyl)-adenine (I) and 9-(2-bromoacetamidobenzyl)adenine (II), two affinity labels. 2. The stoichiometry of the reaction with reagent II is reported: 1 mol reagent is bound per mol inactive enzyme. Amino acid analysis of the 6 N HCl hydrolyzate of the inactive enzyme identified CM-histidine as the main alkylation product. This is the first evidence of the presence of a histidine in the active site region. 3. The alkylation rate and involved amino acid residues were studied for both reagents I and II, at pH 8 and 5.5. The particular reactivity of a lysine near or in the active site is discussed.
| Autori interni: | |
| Autori: | LUCACCHINI A; BERTOLINI AD; RONCA G; SEGNINI D; ROSSI CA |
| Titolo: | AFFINITY LABELING OF HISTIDINE AND LYSINE RESIDUES IN THE ADENOSINE-DEAMINASE SUBSTRATE BINDING-SITE |
| Anno del prodotto: | 1979 |
| Digital Object Identifier (DOI): | 10.1016/0005-2744(79)90057-3 |
| Appare nelle tipologie: | 1.1 Articolo in rivista |
File in questo prodotto:
http://hdl.handle.net/11568/989
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