Isolation and purification of a rat liver-specific antigen from hepatocyte membrane.

Abstract:

:A rat liver-specific antigen (RLSA) solubilized with the nonionic detergent non-anonyl-N-methylglucamide was purified through affinity column chromatography with a monoclonal antibody and by high-performance liquid chromatography with a hydroxylapatite column. The purified RLSA showed a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and its molecular weight was determined to be 105,000 in the presence of 2-mercaptoethanol. The antigen was reactive to the Schiff reagent and contained glucosamine, but not galactosamine, indicating that the RLSA is a glycoprotein containing an asparagine-binding type of sugar chain.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Sato K,Ikeda T,Kawai F,Osada Y

doi

10.1093/oxfordjournals.jbchem.a122134

subject

Has Abstract

pub_date

1987-10-01 00:00:00

pages

933-8

issue

4

eissn

0021-924X

issn

1756-2651

journal_volume

102

pub_type

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