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An endogenous carbohydrate‐binding agglutinin of BHK cells. Purification, specificity and interaction with normal and ricin‐resistant cell lines
Author(s) -
Stojanovic D.,
Hughes R. C.
Publication year - 1984
Publication title -
biology of the cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.543
H-Index - 85
eISSN - 1768-322X
pISSN - 0248-4900
DOI - 10.1111/j.1768-322x.1984.tb00299.x
Subject(s) - baby hamster kidney cell , lectin , agglutinin , biology , hemagglutination , glycoprotein , affinity chromatography , biochemistry , microbiology and biotechnology , sepharose , agglutination (biology) , soybean agglutinin , cell , enzyme , virology , virus , antigen , immunology
Several lectin‐like activities were detected on the surface of unfixed, viable BHK cells by reaction with FITC‐labelled glycosylated albumin derivatives. A prominent surface staining was obtained with the beta‐lactosyl, beta‐N‐acetylgalactosaminyl, alpha‐mannosyl and beta‐N‐acetylglucosaminyl derivatives. Endogenous lectin‐like activities were also detected in BHK cell homogenates by haemagglutination of glutaraldehyde‐fixed rabbit erythrocytes. Haemagglutinating activity was purified by chromatography of sodium deoxycholate‐extracts of BHK cell microsomal fractions on Sepharose 4B and asialofetuin‐Sepharose 4B. A purified agglutinin was eluted from the latter column with 0.2 M thiodigalactoside. The haemagglutination mediated by the purified factor was inhibited by thiodigalactoside, N‐acetylgalactosamine, galactosyl‐beta 1‐4‐N‐acetylglucosamine and several glycoproteins. The purified agglutinin agglutinated trypsinised, fixed normal BHK cells more readily than several ricin‐resistant cell lines. By contrast, a mannose‐binding lectin from rabbit serum reacted equally well with normal and mutant cells. These results are in general agreement with models of cell‐cell adhesion involving the interaction of surface located lectins with carbohydrate sequences of normal BHK cell surface glycoproteins.