l-Glutamine as a Substrate for l-Asparaginase from Serratia marcescens
AUTOR(ES)
Novak, Edward K.
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=285550Documentos Relacionados
- Physical properties of L-asparaginase from Serratia marcescens.
- Purification and Properties of l-Asparaginase from Serratia marcescens1
- Production of Tumor-Inhibitory L-Asparaginase by Submerged Growth of Serratia marcescens1
- Effects on specific antibodies on the catalytic activity of L-asparaginase from Serratia marcescens and Escherichia coli.
- Influence of Dissolved Oxygen Levels on Production of l-Asparaginase and Prodigiosin by Serratia marcescens