The Reversible Inactivation of l-Threonine Dehydratase of Sheep Liver by l-Serine
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چکیده
منابع مشابه
The reversible inactivation of L-threonine hydratase of sheep liver by L-serine.
The action of partially purified L-threonine dehydratase of sheep liver on L-serine has been studied. This enzyme acts on L-serlne as a substrate but is rapidly inactivated in the process, partially at pH 8.9 and more completely at pH 7.2. However, incubation at pH 8.9, with or without L-threonine, leads to a gradual restoration of up to 90% of the original activity. The addition of pyridoxal p...
متن کاملIsolation and Properties of a Homogeneous Preparation of Cystathionine Synthetase-l-serine and L-threonine Dehydratase.
Selim and Greenberg (1, 2) achieved a considerable degree of purification of L-serine dehydratase (L-serine hydro-lyase (deaminating), EC 4.2.1.13) from rat liver and demonstrated that this protein preparation contained the cystathionine-synthesizing activity of the liver (L-serine hydro-lyase (adding L-homocysteine), EC 4.2.1.21). These workers (2) also observed activity of their enzyme prepar...
متن کاملPurification and properties of L-threonine dehydrase of sheep liver.
Materials-L-Threonine, L-serine, and pyridosal-P monohydrate were purchased from the California Corporation for Biochemical Research, a-ketobutyric acid from the Nutritional Biochemical Corporation, pyruvic acid from the Fisher Scientific Company, and DESE-cellulose from Eastman Organic Chemicals. nn-Allothreonine and L-allothreonine were kindly furnished by Dr. Alton iLleister of Tufts Univers...
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1. The activities of l-serine dehydratase and l-serine-pyruvate aminotransferase were determined in rat liver during foetal and neonatal development. 2. l-Serine-pyruvate aminotransferase activity begins to develop in late-foetal liver, increases rapidly at birth to a peak during suckling and then decreases at weaning to the adult value. 3. l-Serine dehydratase activity is very low prenatally, ...
متن کاملRat liver L-threonine dehydrogenase.
L-threonine dehydrogenase (E.C.1.1.1.103) catalyzes the NAD+-dependent transformation of Lthreonine to 2-amino 3-0x0-butyric acid, which spontaneously loses CO2 with the final production of aminoacetone ( 1) The enzyme is present in several microorganisms as well as in the liver of vertebrates (2-6). We studied some properties of the rat liver enzyme, showing that the activity was strongly inhi...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1968
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)99312-9