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These glycoproteins were shown by specific labelling and enzyme digestion of cells to be the major components of the trypanosome surface coat. Each glycoprotein consisted of a single polypeptide chain having an apparent molecular weight of 65000 (as measured by SDS-polyacrylamide gel electrophoresis) and containing around 600 amino acid and 20 monosaccharide residues. Preliminary structural studies indicated large changes in amino acid sequence dispersed over a considerable length of the polypeptide chain. Proteolytic activity was demonstrated in semi-purified trypanosome extracts, providing one reason for the heterogeneity sometimes observed in surface glycoprotein antigen preparations.<\/jats:p>","DOI":"10.1017\/s003118200004717x","type":"journal-article","created":{"date-parts":[[2009,6,5]],"date-time":"2009-06-05T16:57:35Z","timestamp":1244221055000},"page":"393-417","source":"Crossref","is-referenced-by-count":707,"title":["Identification, purification and properties of clone-specific glycoprotein antigens constituting the surface coat of<i>Trypanosoma brucei<\/i>"],"prefix":"10.1017","volume":"71","author":[{"given":"G. A. 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