Author/Authors
B. Ganesh Bhat، نويسنده , , Ping Wang، نويسنده , , Ji-Hyeon Kim، نويسنده , , Tracy M. Black، نويسنده , , Tal M. Lewin، نويسنده , , Frederick T. FiedorekJr.، نويسنده , , Rosalind A. Coleman، نويسنده ,
DocumentNumber
1601476
Title Of Article
Rat sn-glycerol-3-phosphate acyltransferase: molecular cloning and characterization of the cDNA and expressed protein
شماره ركورد
11686
Latin Abstract
Rat mitochondrial glycerol-3-phosphate acyltransferase (GPAT) cDNA was cloned and characterized. We identified a cDNA containing an open reading frame of 828 amino acids that had an 89% homology with the coding region of the previously characterized mouse mitochondrial GPAT and a predicted amino acid sequence that was 96% identical. The rat 5′ UTR was only 159 nucleotides, in contrast to the 926 nucleotide 5′ UTR of the mouse cDNA and had an internal deletion of 167 nucleotides. GPAT was expressed in Sf21 insect cells, and specific inhibitors strongly suggest that, like the Escherichia coli GPAT, the recombinant mitochondrial GPAT and the mitochondrial GPAT isoform in rat liver contain critical serine, histidine, and arginine residues
From Page
415
NaturalLanguageKeyword
triacylglycerol , Glycerolipid synthesis , Diacylglycerol metabolism , Glycerol-3-phosphate acyltransferase
JournalTitle
Studia Iranica
To Page
423
To Page
423
Link To Document