Glutamic-Glycine Transaminase from Rat Liver
نویسندگان
چکیده
منابع مشابه
Glutamic-glycine Transaminase from Rat Liver.
.ilthough there is ample evidence for the existence of many different transaminases, the lack of progress in the separation of more individually specific transaminases has been lamented by reviewers for a number of years. Transaminations involving glycine or glyoxylate have been studied extensively in crude preparations of animal (1, 2), plants (3), and microorganisms (4), as well as with purif...
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Aspartate and glutamate react instantaneously with the pyridoxal form of the pig heart glutamic aspartic transaminase (1) to yield the corresponding keto acid, converting the enzymebound pyridoxal phosphate to bound pyridoxamine phosphate (2). Other amino acids such as methionine sulfoxide, methionine sulfone, and alanine react much more slowly with the enzyme, but the reaction itself appears t...
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The hepatic plasma membrane fatty acid-binding protein (h-FABPPM) and the mitochondrial isoenzyme of glutamic-oxaloacetic transaminase (mGOT) of rat liver have similar amino acid compositions and identical amino acid sequences for residues 3-24. Both proteins migrate with an apparent molecular mass of 43 kDa on SDS/polyacrylamide gel electrophoresis, have a similar pattern of basic charge isome...
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Liver tissue of the rat, fixed in glutaraldehyde and formaldehyde, was incubated in a medium which consisted of 20 mML-aspartic acid, 2 mM alpha-ketoglutaric acid, 50 mM imidazole and 6 mM lead nitrate at pH 7.2-7.4. The electron-opaque precipitates, due to glutamic oxalacetic transaminase activity in liver cells, were found to be localized to the cristae and surface membranes of the mitochondr...
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With the discovery that pyridoxal phosphate and pyridoxamine phosphate were cofactors for enzymatic transamination, it was proposed that the reaction was biphasic, involving first an amino group transfer from the amino acid substrate to enzymebound pyridoxal phosphate, followed by a transfer of the amino group to the keto acid substrate (for review, see (1)). With the availability of a highly p...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1964
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)51703-8