Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.4.1.2 (glutamate dehydrogenase)
 4,380 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Four cytoplasmically synthesized rat liver mitochondrial enzymes, located either as soluble enzymes in the mitochondrial matrix (L-glutamate dehydrogenase and malate dehydrogenase or in the intermembrane space (sulfite oxidase) or as an integral membrane protein located on the matrix face of the inner mitochondrial membrane (D-beta-hydroxybutyrate dehydrogenase), were all shown to be synthesized as precursors larger than their mature counterparts by 1000-6000 daltons. These larger forms were detected in vitro, in a cell-free protein synthesizing system programmed with either total rat liver RNA or with RNA isolated from free polysomes or with free polysomes, and in vivo, in the two cases that were investigated (L-glutamate dehydrogenase and D-beta-hydroxybutyrate dehydrogenase), by pulse labeling of Buffalo rat liver cells in culture. The intracellular site of synthesis of all four mitochondrial enzymes was shown to be primarily on free polysomes and not on membrane-bound polysomes.
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PMID:Rat liver L-glutamate dehydrogenase, malate dehydrogenase, D-beta-hydroxybutyrate dehydrogenase, and sulfite oxidase are each synthesized as larger precursors by cytoplasmic free polysomes. 706 82

A detailed subfractionation of the non-pregnant porcine corpus luteum (CL) was performed employing differential centrifugation. Marker enzyme assays (i.e., lactate dehydrogenase for the cytosol, NADPH-cytochrome P450 reductase for the endoplasmatic reticulum, catalase (CAT) for peroxisomes, glutamate dehydrogenase for the mitochondrial matrix and acid phosphatase for lysosomes) in all subfractions obtained exhibited a pattern of distribution similar to that observed with rat liver. These subfractions should be useful in connection with many types of future studies. In disagreement with previous biochemical and morphological studies, peroxisomes (identified on the basis of catalase activity and by Western blotting of catalase and of the major peroxisomal membrane protein (PMP-70)) sedimented together with mitochondria (i.e., at 5000 x g(av) for 10 min) and not in the post-mitochondrial fraction prepared at 30,000 x g(av) for 20 min by Peterson and Stevensson. No other classical peroxisomal enzymes were detectable in the porcine ovary, raising questions concerning the function of peroxisomes in this organ. Furthermore, UDP-glucuronosyltransferase (UGT), generally considered to be an integral membrane protein anchored in the endoplasmatic reticulum, was recovered in both the cytosolic (i.e., the supernatant after centrifugation at 50,000 x g(av) for 1h) and the microsomal fraction of the porcine corpus luteum, even upon further centrifugation of the former. In contrast, UGT sediments exclusively in the microsomal fraction upon subfractionation of the liver and ovary from rat.
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PMID:Detailed analytical subcellular fractionation of non-pregnant porcine corpus luteum reveals peroxisomes of normal size and significant UDP-glucuronosyltransferase activity in the high-speed supernatant. 1472 50