Glutaminase from Pig Renal Cortex
نویسندگان
چکیده
منابع مشابه
Glutaminase from Pig Renal Cortex
A method for preparing highly purified glutaminase (EC 3.5.1.2, L-glutamine amidohydrolase) from pig renal cortex is described. The main steps consist of sodium sulfate fractionation followed by alternative solubilization by dialysis against Tris-HCI buffer and precipitation with phosphateborate. The linal enzyme preparation contains no impurities which could be detected by sucrose gradient cen...
متن کاملGlutaminase from pig renal cortex. II. Activation by inorganic and organic anions.
The Tris-HCl and phosphate-borate forms of glutaminase (EC 3.5.1.2, L-glutamine amidohydrolase) are both activated and protected from inactivation by phosphate and carboxylic acids. The Tris-HCI enzyme is less sensitive to this activation, but more sensitive to glutamate inhibition than the phosphate-borate enzyme. Plots of activity against concentration of activating anions are generally sigmo...
متن کاملGlutamine synthesis from aspartate in guinea-pig renal cortex.
1. Glutamine was found to be the main carbon and nitrogen product of the metabolism of aspartate in isolated guinea-pig kidney-cortex tubules. Glutamate, ammonia and alanine were only minor products. 2. Carbon-balance calculations and the release of 14CO2 from [U-14C]aspartate indicate that oxidation of the aspartate carbon skeleton occurred. 3. A pathway involving aspartate aminotransferase, g...
متن کاملRenal Glutaminase Activities in Vitamin
Glutamine has been implicated in the functioning of the central nervous system (l), in muscle metabolism (a), in transamination (3), in detoxification (4), and as a precursor of urinary ammonia (5). An excellent review of these and other possible r&es of glutamine in metabolism has been presented by Archibald (6). It would seem that glutamine acts as a mobile reserve of ammonia and glutamic aci...
متن کاملProperties and submitochondrial localization of pig and rat renal phosphate-activated glutaminase.
Two pools of phosphate-activated glutaminase (PAG) were separated from pig and rat renal mitochondria. The partition of enzyme activity corresponded with that of the immunoreactivity and also with the postembedding immunogold labeling of PAG, which was associated partly with the inner membrane and partly with the matrix. The outer membrane was not labeled. PAG in intact mitochondria showed enzy...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1970
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)63179-5