title: L-glutamine as a substrate for L-asparaginase from Serratia marcescens.
abstract: l-Asparaginase from Serratia marcescens was found to hydrolyze l-glutamine at 5% of the rate of l-asparagine hydrolysis. The ratio of the two activities did not change through several stages of purification, anionic and cationic polyacrylamide disk gel electrophoresis, and partial thermal inactivation. The two activities had parallel blood clearance rates in mice. l-glutamine was found to be a competitive inhibitor of l-asparagine hydrolysis. A separate l-glutaminase enzyme free of l-asparaginase activity was separated by diethylaminoethyl-cellulose chromatography.
mesh_terms: D000645:Ammonium Sulfate; D000818:Animals; D001215:Asparaginase / Q000097:blood / Q000302:isolation & purification / Q000378:metabolism*; D001216:Asparagine / Q000378:metabolism; D011232:Chemical Precipitation; D002848:Chromatography, DEAE-Cellulose; D004589:Electrophoresis, Disc; D004926:Escherichia coli / Q000201:enzymology; D005260:Female; D005972:Glutaminase / Q000097:blood / Q000302:isolation & purification / Q000378:metabolism; D005973:Glutamine / Q000378:metabolism*; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D051379:Mice; D008809:Mice, Inbred C3H; D012706:Serratia marcescens / Q000201:enzymology* / Q000254:growth & development; D013053:Spectrophotometry; D013237:Stereoisomerism
chemical_list: D005973:Glutamine; D001216:Asparagine; D001215:Asparaginase; D005972:Glutaminase; D000645:Ammonium Sulfate