منابع مشابه
Substrate specificity and aspects of deamination catalyzed by rabbit muscle 5'-adenylic acid aminohydrolase.
A total of 24 nucleotides were examined as substrates for 5’-AMP aminohydrolase (EC 3.5.4.6). The following nucleotides were deaminated at the indicated maximum velocity relative to AMP (100): adenosine 5’-phosphoramidate (73), iV-methyl-AMP (ZO), dAMP (18), adenosine 5’-monosulfate (13), adenosine (l), and ADP (1). Other substrates for which maximum velocities were not determined included W-et...
متن کامل5’-adenylic Acid Deaminase
In 1928, Schmidt (1) first described the presence of 5’-adenylic acid deaminase in muscle. He succeeded in separating this enzyme from adenosine deaminase and in isolating inosinic acid and ammonia as products of the reaction. He also reported that it specifically deaminated 5’-adenylic acid. In 1947, Kalckar (2) described two methods for the preparation of this enzyme and introduced a spectrop...
متن کامل5’-adenylic Acid Deaminase
In 1928, Schmidt (1) first described the presence of 5’-adenylic acid deaminase in muscle. He succeeded in separating this enzyme from adenosine deaminase and in isolating inosinic acid and ammonia as products of the reaction. He also reported that it specifically deaminated 5’-adenylic acid. In 1947, Kalckar (2) described two methods for the preparation of this enzyme and introduced a spectrop...
متن کاملThe purification and properties of 5-adenylic acid deaminase from muscle.
Schmidt (1) was the first to extract an enzyme catalyzing the deamination of 5-adenylic acid. He demonstrated the presence of adenosine and adenylic acid deaminases in NaHC03 extracts of saline-washed minced rabbit muscle. Purification of the preparation by adsorption with alumina removed the adenosine deaminase, thus demonstrating that deamination of adenylic acid and adenosine is catalyzed by...
متن کاملAn improved purification, crystallization, and some properties of rabbit muscle 5'-adenylic acid deaminase.
A rapid method for the preparation of crystalline 5’-adenylic acid deaminase from rabbit skeletal muscle is presented. The enzyme remains bound to cellulose phosphate under conditions at which apparently no other proteins are bound; thus it was possible to develop, in essence, a one-step method for its purification. The crystalline preparation is homogeneous as indicated by its elution profile,...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1974
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)42027-9