Effect of non-enzymatic desamidation of gamma-globulin on its properties and biological activity

During incubation of gamma-globulin preparations under conditions similar to physiological ones within 28 days (0.9% NaCl, pH 7.0, 37 degrees) as well as during storage at 3-10 degrees within 36 months gradual nonenzymatic deamidation of the protein occurred mainly due to hydrolysis of readily acces...

Full description

Saved in:

Bibliographic Details
Published in:	Voprosy meditsinskoi khimii Vol. 31; no. 4; p. 104
Main Authors:	Lukash, A I, Shepelev, A P, Pushkina, N V, Tsybul'skiĭ, I E, Al'perovich, D V
Format:	Journal Article
Language:	Russian
Published:	Russia (Federation) 01-07-1985
Subjects:	Amides - analysis Ammonia - analysis Deamination Drug Stability Drug Storage gamma-Globulins - analysis gamma-Globulins - immunology Humans Immunization, Passive Measles - prevention & control Precipitin Tests Protein Conformation
Online Access:	Get more information
Tags:	Add Tag No Tags, Be the first to tag this record!

Description
Summary:	During incubation of gamma-globulin preparations under conditions similar to physiological ones within 28 days (0.9% NaCl, pH 7.0, 37 degrees) as well as during storage at 3-10 degrees within 36 months gradual nonenzymatic deamidation of the protein occurred mainly due to hydrolysis of readily accessible amide groups (asparagine). Fluorescence of the preparations decreased gradually in the course of deamidation; it constituted for 82% of the initial value after incubation during 28 days. Immunological activity of the gamma-globulin, which lost 19.6% of amide groups, was decreased by 34%; alteration in the amidation by 45.1% was accompanied by a decrease in active antibodies concentration by 92.3%. Nonenzymatic deamidation may be responsible for conformational alterations and inactivation of gamma-globulin.
ISSN:	0042-8809