منابع مشابه
Kinetics of Beef Heart Glutamic-alanine Transaminase.
It has now been clearly established that pyridoxal phosphate serves as the coenayme of many transaminases. Several lines of evidence have indicated that the coenzyme acts alternately as acceptor and donar of amino groups, shuttling between the aldehydic (pyridoxal phosphate) and amino (pyridoxamine phosphate) forms (2-11). However, a detailed study of the kinetics of the transaminase reaction w...
متن کاملTransaminase activity in human blood.
Enzymatic transamination consists of the enzyme catalyzed reversible transfer of the alpha amino nitrogen of an amino acid to an alpha-keto acid with the synthesis of a second amino acid and a second alpha-keto acid. Enzymes catalyzing different transamination reactions are found widely distributed in animal tissues and have been shown to change in activity in some tissues during disease (1-3)....
متن کاملTransaminase Activity in Neurospora crassa
It is now believed that the amino groups of isoleucine and valine are accepted by their respective carbon chains during biosynthesis via a transamination. Most of the evidence for this hypothesis has been derived from experiments on isoleucineless and valineless mutants of Escherichia coli and Neurospora crassu (l-4). It is not positively established whether this transamination step can be medi...
متن کاملTransaminase activity after codeine administration.
THE quantitative and serial changes that occur in serum glutamic-oxaloacetic transaminase (SGOT) activity during the course of a myocardial infarction are well recognized. Changes in SGOT activity have been observed in other diseases such as hepatitis and pancreatitis (Wroblewski and LaDue, '955; Chinsky, Shmagranoff and Sherry, 1956) and after the administration of drugs such as chlorpromazine...
متن کاملInhibition of tyrosine transaminase activity by norepinephrine.
The neurotransmitter, norepinephrine, and structurally related primary catecholamines inhibited rat hepatic tyrosine transaminase activity (L-tyrosine:2-oxoglutarate aminotransferase, EC 2.6.1.5) in vitro. The inhibition was competitive with pyridoxal 5’-phosphate cofactor and an “apparent” I& of 4.0 x 10-e M was determined. (The “apparent” K,,, was 6.6 X 10-T M.) Those amines which were associ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1940
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)73021-4