Molecular cloning of a cDNA for rat hepatic glutaminase. Sequence similarity to kidney-type glutaminase.

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Molecular cloning of a cDNA for rat hepatic glutaminase. Sequence similarity to kidney-type glutaminase.

Mammalian liver possesses a unique isozyme of phosphate-activated glutaminase which plays an important role in the regulation of glutamine catabolism. Antibodies to hepatic glutaminase were used to screen a lambda gt11 rat liver cDNA library. One cDNA to hepatic glutaminase was identified. Changes in the relative abundance of hepatic glutaminase mRNA were determined by hybridization to this cDN...

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Hepatic glutaminase expression: relationship to kidney-type glutaminase and to the urea cycle.

Glutamine functions as a major transport form of nitrogen and carbon within the body. In the liver, glutamine is hydrolyzed by a unique liver-type, phosphate-activated glutaminase, and the end products of hepatic glutamine catabolism are glucose and urea. Other tissues possess a different, kidney-type, glutaminase isozyme. The predicted amino acid sequences for the two glutaminases show a high ...

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Inhibition by glutamate of phosphate-dependent glutaminase of rat kidney.

A membrane-associated form of phosphate-dependent glutaminase was derived from sonicated mitochondria and purified essentially free of gamma-glutamyl transpeptidase activity. Increasing concentrations of phosphate cause a sigmoidal activation of the membrane-bound glutaminase. Phosphate also causes a similar effect on the rate of glutaminase inactivation by the two affinity labels, L-2-amino-4-...

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The subcellular localization of glutaminase isoenzymes in rat kidney cortex.

The subcellular localization of the isoenzymes of glutaminase has been studied in rat renal cortex. Differential and sucrose density centrifugation techniques demonstrated a mitochondrial localization for phosphate-dependent glutaminase. Fractionation of isolated mitochondria by digitonin and by sonication revealed a matrix localization for phosphate-dependent glutaminase, a finding in agreemen...

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Complexity and species variation of the kidney-type glutaminase gene.

Increased expression of rat kidney-type glutaminase (KGA) during metabolic acidosis results from selective mRNA stabilization. This process is mediated by an 8-base AU-sequence that functions as a pH-response element (pHRE). LLC-PK1-FBPase+ cells, a pH-responsive porcine kidney cell line, express four distinct GA mRNAs. RNase H mapping indicated that three of the GA mRNAs are generated by use o...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1990

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(18)86993-9