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PMID: 438168 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Effect of trypsin on the cell surface proteins of hepatoma tissue culture cells. Characterization of a carbohydrate-rich glycopeptide released from a calcium binding membrane glycoprotein.

The Journal of biological chemistry ·Vol. 254 ·No. 10 ·1979-05-25 ·Pages 3935-46

Baumann H, Doyle D

Abstract

Concentrations of trypsin that bring about aggregation of hepatoma tissue culture (HTC) cells also release from the cell surface an Mr = 55,000 glycopeptide fragment. This glycopeptide fragment also accumulates in the medium, including serum-free medium, as a normal consequence of membrane protein turnover. The trypsin-released glycopeptide is labeled when cells are grown in the presence of fucose or leucine before treatment of the cells with the protease. Similarly, the glycopeptide fragment can be labeled by reacting cells in situ by lactoperoxidase-catalyzed radioiodination or by tritiated borohydride reduction of cells treated first with neuraminidase and galactose oxidase. The tryptic glycopeptide fragment was purified by concanavalin A-Sepharose chromatography, and hydroxyapatite chromatography in the presence of dodecyl sulfate. The amino acid and carbohydrate composition was determined, as was the sensitivity of the purified glycopeptide to a variety of endo- and exoglycosidases. The purified glycopeptide contains an average of 17 sialic acid residues and hence, shows charge heterogeneity after electrophoresis in isoelectric focusing gels. The charge heterogeneity can be eliminated completely by treatment with neuraminidase. The glycopeptide after this treatment is homogeneous. The trypsin-sensitive membrane glycoprotein which is the source of the Mr = 55,000 glycopeptide was identified by two-dimensional gel electrophoretic analysis of labeled cells, treated or not treated with trypsin. This glycoprotein, which has an apparent molecular weight of 85,000 and forms a homodimer in the presence of calcium ions, was purified and its identity as the parent of the Mr = 55,000 glycopeptide was confirmed by showing that the same Mr = 55,000 fragment was released by trypsin from the purified glycoprotein as was released from the intact cells.

MeSH Terms
Amino Acids/analysis Animals Calcium/metabolism Carbohydrates/analysis Cell Aggregation Cell Line Glycopeptides/analysis Glycoproteins/metabolism Liver Neoplasms, Experimental Macromolecular Substances Membrane Proteins/metabolism Molecular Weight Neoplasm Proteins/metabolism Peptide Fragments/analysis Rats Trypsin
Chemicals
Amino Acids Carbohydrates Glycopeptides Glycoproteins Macromolecular Substances Membrane Proteins Neoplasm Proteins Peptide Fragments Trypsin Calcium
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Baumann H
Doyle D
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1979-05-25
Pages
3935-46
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
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