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- W184226509 abstract "The phosphate-dependent glutaminase is asymmetrically associated with the matrix surface of the inner membrane of rat renal mitochondria. The glutaminase contained within intact mitochondria consists of two peptides that are structurally related. However, in vitro translation of renal poly(A/sup +/)RNA yields a 72 kDa protein that is precipitated by glutaminase specific IgG. HTC hepatoma cells and primary cultures of renal proximal tubular cells were used to determine if the 72 kDa protein is a precursor of the mitochondrial glutaminase. When the cells were incubated with (/sup 35/S)methionine for < 3 min. the predominant immunoprecipitable glutaminase has a M/sub r/=72 kDa. With longer periods of incubation, labeled peptides of M/sub r/ = 68 and 65 kDa were also immunoprecipitated. When cells were pulse labeled in the presence of 5 ..mu..M CCCP, a mitochondrial uncoupler, only the 72 kDa protein is formed. When chased with 10 mM methionine and 10 mM cystamine, an antagonist of CCCP, the 72 kDa protein is processed to the 68 and 65 kDa peptides. This process occurs rapidly at 37/sup 0/C, but is slowed considerably at 10/sup 0/C. Quantitative fluorographic analysis of the immunoprecipitated and separated peptides should establish the temporal sequence and kinetics of formation ofmore » the processed forms of the glutaminase. Further studies will be conducted to determine the structural difference between the two peptides and their functional significance.« less" @default.
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- W184226509 date "1987-05-01" @default.
- W184226509 modified "2023-09-22" @default.
- W184226509 title "Biosynthesis and processing of mitochondrial glutaminase" @default.
- W184226509 hasPublicationYear "1987" @default.
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