منابع مشابه
Rat 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...
متن کاملCalcium-cadmium interaction on L-threonine intestinal transport.
Cadmium is a highly toxic metal that can damage a number of organs including the gastrointestinal tract. It has been shown that cadmium partially reduces L-threonine intestinal absorption probably by binding to membrane proteins which pertain to active transport systems or are functionally related to them. Calcium, however, is an essential element in a wide variety of cellular activities. The a...
متن کاملOn the N-methyl-L-threonine residue in stendomycin.
Sir: In a previous communication^ to this Jour nal, the isolation of N-methyl-L-threonine from acid hydrolysates of stendomycin2~4) was briefly mentioned. We wish to report here some experiments that led to the final assignment of the configuration for this amino acid with two centers of asymmetry. The specific rotation of the N-methyl amino acid from stendomycin was in good agreement with the ...
متن کاملL-threonine in the treatment of spasticity.
Preclinical data indicate that the administration of the amino acid L-threonine increases glycine levels in rat spinal cord. In order to investigate glycinergic mechanisms in spasticity, and other signs of the upper motor syndrome, we gave 4.5 and 6.0 g/day of L-threonine to 18 patients with familial spastic paraparesis (FSP) according to a double-blind, crossover protocol. The response to trea...
متن کاملBiodegradative L-threonine deaminase of Salmonella typhimurium.
The threonine deaminase formed under anaerobic conditions by Salmonella typhimurium is induced by l-serine and l-threonine, is catabolite repressible, requires cyclic adenosine 3',5'-monophosphate for its synthesis and adenylic acid for optimal activity, and is immunologically different from biosynthetic threonine deaminase.
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ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1971
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.35.2089