منابع مشابه
5’-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 کاملAdenylic Acid Deaminase of Rat Liver.
The existence of a specific deaminase in muscle tissue for the deamination of adenylic acid (AMP) was firmly established by its crystallization and characterization (l-3). Whether hepatic tissue also had a specific AMP deaminase appeared less certain. For instance, Conway and Cooke (4) believed that the deamination of AMP in rabbit liver was preceded by dephosphorylation. On the other hand, Kut...
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: 1957
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)70779-5