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    POWERFUL INHIBITOR OF GUANINE DEAMINASE

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    The synthesis of 9-(p-carbetoxyphenyl) guanine is reported. The assays carried out on guanine deaminase from rat and rabbit liver and pig brain show that this compound is a powerful inhibitor. The compound has a Ki = 5 uM for the enzyme from pig brain. The use of the inhibitor for the synthesis of a specific adsorbent for guanine deaminase was studied

    EFFECTS OF SUBSTITUTED 1,2,3-TRIAZOLES ON ADENOSINE-DEAMINASE, GUANINE DEAMINASE AND XANTHINE-OXIDASE

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    The action of some known and new synthesized substituted 1,2,3-triazoles on adenosine deaminase, guanine deaminase and xanthine oxidase was studied. The effect of substituents in 1, 4 and 5 positions was studied and discussed. The presence of a carboxamido group in 4 position seems to be essential in the binding to adenosine deaminase

    AFFINITY LABELING OF HISTIDINE AND LYSINE RESIDUES IN THE ADENOSINE-DEAMINASE SUBSTRATE BINDING-SITE

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    1. 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

    EVIDENCE OF SOLUBLE-PROTEINS BINDING ADRIAMYCIN BY AFFINITY CHROMATOGRAPHY

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    The presence of various tissues of soluble proteins binding adriamycin is evidenced by affinity chromatography
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