Monoclonal Antibody GOM-2 Binds to Blood Group B-Le(y) Active Glycolipid Antigens on Human Gastric Cancer Cells, KATO-III

Overview

Journal Glycoconj J

Publisher Springer

Specialties Biochemistry
Endocrinology

Date 1992 Apr 1

PMID 1344715

Authors

S Sueyoshi

H Nagakura

A Kato

S UETSUKI

Y Nakayama

M Adachi

Affiliations

Soon will be listed here.

Abstract

The antigen structure of a mouse monoclonal antibody, GOM-2, established by immunization with KATO-III human gastric cancer cells, was examined. GOM-2 reactive glycolipids were prepared from KATO-III cells and treated with endoglycoceramidase. Structural studies of ten GOM-2 reactive oligosaccharides by a combination of glycosidase digestions, methylation, and affinity chromatography on an Ulex europeus agglutinin I (UEA-I) column revealed that nine of them had a Y-related B-active difucosylated determinant (B-Le(y)) and one had a B-active determinant. Affinity chromatography of the purified and modified oligosaccharides on an immobilized GOM-2 column demonstrated that GOM-2 has a novel binding specificity: it binds tightly to the biantennary structure carrying the B-Le(y) determinant at the termini or the branched structure carrying the B-Le(y) structure at two nonreducing termini.

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