Immunochemical study of modified forms of L-asparaginase

Certain catalytic and immunological properties of L-asparaginase modified by polyglucin were studied. It was shown that the modified forms of L-asparaginase maintained high catalytic activity (Km 0.80.10(-5)-1.89.10(-5) M) and at the same time appeared to be more resistant to inactivation under the...

Full description

Saved in:

Bibliographic Details
Published in:	Antibiotiki i meditsinskaia biotekhnologiia = Antibiotics and medical biotechnology Vol. 32; no. 11; p. 846
Main Authors:	Iulaev, M F, Ivnitskiĭ, D M, Kashkin, A P, Bogdanova, T Ia, Korsakova, A S
Format:	Journal Article
Language:	Russian
Published:	Russia (Federation) 01-11-1987
Subjects:	Animals Antibodies - metabolism Asparaginase - antagonists & inhibitors Asparaginase - immunology Asparaginase - pharmacokinetics Catalysis Dextrans - immunology Dextrans - pharmacokinetics Drug Interactions Enzymes, Immobilized - antagonists & inhibitors Enzymes, Immobilized - immunology Enzymes, Immobilized - pharmacokinetics Escherichia coli - enzymology Immunization Immunochemistry Rabbits
Online Access:	Get more information
Tags:	Add Tag No Tags, Be the first to tag this record!

Description
Summary:	Certain catalytic and immunological properties of L-asparaginase modified by polyglucin were studied. It was shown that the modified forms of L-asparaginase maintained high catalytic activity (Km 0.80.10(-5)-1.89.10(-5) M) and at the same time appeared to be more resistant to inactivation under the effect of antibodies.
ISSN:	0233-7525