Generation of aspartate aminotransferase multiple forms by deamidation
نویسندگان
چکیده
منابع مشابه
Photoinactivation of aspartate aminotransferase.
The cofactor pyridoxal 5’-phosphate bound through an aldimine linkage to lysine residues of the enzyme aspartate amiuotransferase is very stable to irradiation with light of 420 nm. The catalytic function of the enzyme exposed to light absorbed by the cofactor remains unaffected, indicating that pyridoxal 5’-phosphate is not an efficient active site photosensitizer for this aminotransferase. Th...
متن کاملAcylation of aspartate aminotransferase.
1. Acetylation of aspartate aminotransferase from pig heart inhibits completely the enzymic activity when the coenzyme is in the amino form (pyridoxamine phosphate) or when the coenzyme has been removed, but not when the coenzyme is in the aldehyde form (pyridoxal phosphate). 2. The group the acylation of which is responsible for the inhibition has been identified with the in-amino group of a l...
متن کاملAspartate: 2-oxoglutarate aminotransferase from trichomonas vaginalis. Identity of aspartate aminotransferase and aromatic amino acid aminotransferase.
Aspartate: 2-oxoglutarate aminotransferase from the anaerobic protozoon Trichomonas vaginalis was purified to homogeneity and characterized. It is a dimeric protein of overall Mr approx. 100000. Only a single isoenzyme was found in T. vaginalis. The overall molecular and catalytic properties have features in common with both the vertebrate cytoplasmic and mitochondrial isoenzymes. The purified ...
متن کاملOptimization of methods for aspartate aminotransferase and alanine aminotransferase.
Conditions for accurate measurement of catalytic activity of aspartate aminotransferase and alanine aminotransferase in human serum have been reinvestigated. The basic variables (kind of buffer, buffer concentration, pH, ion effects, and the influence of pyridoxal-5-phosphate) can now be considered optimized. On this basis, the kinetic parameters of both aminotransferases were determined, i.e.,...
متن کاملAffinity labeling of aspartate aminotransferase isozymes by bromopyruvate.
Incubation with bromopyruvate did not cause appreciable inactivation of either supernatant or mitochondrial isozyme of aspartate aminotransferase from pig heart. In the presence of either L-cysteine sulfinate or L-aspartate, however, bromopyruvate rapidly inactivated both isozymes. Bromopyruvate also acted as a keto acid substrate in the conversion of the pyridoxamine form of both enzymes to th...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1979
ISSN: 0264-6021
DOI: 10.1042/bj1770121