منابع مشابه
L-triiodothyronine and L-reverse-triiodothyronine generation in the human polymorphonuclear leukocyte.
Extrathyroidal monodeiodination of l-thyroxine (T(4)) is the principal source of l-triiodothyronine (T(3)) and l-reverse-triiodothyronine (rT(3)) production. To define some of the cellular factors involved, we examined T(3) and rT(3) generation from added nonradioactive T(4) in human polymorphonuclear leukocytes, using radioimmunoassays to quantify the T(3) and rT(3) generated. Under optimum in...
متن کاملA rat-tissue aminotransferase acting on L-tyrosine O-sulphate.
1. Rat tissues have been shown to possess an aminotransferase that is active towards l-tyrosine O-sulphate and dependent on 2-oxoglutarate and pyridoxal phosphate. 2. Kidney, liver and pancreas have the greatest activity and the enzyme is localized mainly in the mitochondrial fraction in the liver and kidney cell. 3. The enzyme was shown to be distinct from l-tyrosine-2-oxoglutarate aminotransf...
متن کاملIncreased liver L-serine-pyruvate aminotransferase activity under gluconeogenic conditions.
Rat liver l-serine-pyruvate aminotransferase activity exceeds markedly the normal adult value (a) in the neonatal period, (b) after glucagon injection and (c) after alloxan injection, observations that reinforce the suggestion from comparative findings that the aminotransferase has a role in gluconeogenesis. Some findings, however, argue in favour of l-serine dehydratase as the enzyme of glucon...
متن کاملProperties of an Aminotransferase of Pea (Pisum sativum L.).
A transaminase (aminotransferase, EC 2.6.1) fraction was partially purified from shoot tips of pea (Pisum sativum L. cv. Alaska) seedlings. With alpha-ketoglutarate as co-substrate, the enzyme transaminated the following aromatic amino acids: d,l-tryptophan, d,l-tyrosine, and d,l-phenylalanine, as well as the following aliphatic amino acids: d,l-alanine, d,l-methionine, and d,l-leucine. Of othe...
متن کاملEnzymatic synthesis of L-tert-leucine with branched chain aminotransferase.
In this study, we demonstrated the asymmetric synthesis of L-tert-leucine from trimethylpyruvate using branchedchain aminotransferase (BCAT) from Escherichia coli in the presence of L-glutamate as an amino donor. Since BCAT was severely inhibited by 2-ketoglutarate, in order to overcome this here, we developed a BCAT/aspartate aminotransferase (AspAT) and BCAT/AspAT/pyruvate decarboxylase (PDC)...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1973
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)44286-5