title: The turnover of lysosomal glycosylasparaginase in rat liver.
abstract: Rat liver glycosylasparaginase (N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine amidohydrolase (EC 3.5.1.26) was irreversibly inhibited in vitro by the asparagine analogue 5-diazo-4-oxo-L-norvaline (DONV). Following the abolition of this lysosomal hydrolase by DONV in rats, the enzyme activity in liver recovered exponentially. Assuming a zero order rate of protein synthesis, the half-life of the glycosylasparaginase in rat liver was measured to be 2 days.
authors: Department of Molecular and Cell Biology, Pennsylvania State University, University Park.
authors: O K
authors: OK
authors: Tollersrud
authors: S H
authors: SH
authors: Hofmann
authors: N N
authors: NN
authors: Aronson
mesh_terms: D000581:Amidohydrolases / Q000378:metabolism*; D000622:Aminolevulinic Acid / Q000031:analogs & derivatives / Q000494:pharmacology; D000818:Animals; D001227:Aspartylglucosylaminase / Q000378:metabolism*; D006207:Half-Life; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008247:Lysosomes / Q000201:enzymology*; D051381:Rats
chemical_list: C002199:5-diazo-4-oxonorvaline; D000622:Aminolevulinic Acid; D000581:Amidohydrolases; D001227:Aspartylglucosylaminase