Nucleotide Transphosphorylases from Liver
نویسندگان
چکیده
منابع مشابه
Nucleotide Transphosphorylases from Liver*
Adenylate kinase activity has been found in yeast and various animal tissues such as muscle, liver, heart, spleen, brain (2), and erythrocytes (3). However, only the enzyme from rabbit muscle has been studied extensively and it has been crystallized by Noda and Kuby (4). Recent reports by Strominger et aZ. (5) and Heppel et al. (6) on the nucleoside monophosphate kinases of calf liver indicate ...
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Procedures are described for the isolation, in crystalline form, of the adenylate kinases from autopsy samples of human muscle and from human liver. Weight average molecular weights were determined by sedimentation equilibrium to be 22,000 (+/- 700) and 25,450 (+/- 160) for the human muscle and liver isoenzymes, respectively. By sodium dodecyl sulfate-polyacrylamide gel electrophoresis, their m...
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The isolation of the crystalline enzymes, adenosine triphosphate-creatine transphosphorylase (1) and adenosine triphosphate-adenosine 5’-phosphate transphosphorylase (2), made possible a comparative approach to the general problem of the mechanism of action of the adenosine triphosphate transphosphorylases. The present series of papers extends earlier studies from this laboratory on these enzym...
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The classical studies of Dutton and Storey (1) have shown that liver microsomes catalyze the transfer of glucuronic acid from uridine diphosphate glucuronic acid to phenols. In an attempt to detect a reaction between uridine diphosphate glucuronic acid and uridine diphosphate N-acetylglucosamine, the effect of the latter on phenol glucuronidation was tested. It was expected that a reaction betw...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1961
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)63306-5