作者: Jose Hector Aguilar
DOI: 10.1016/S0021-9258(19)43678-8
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摘要: Abstract Glycopeptides from soluble rat skin collagen were prepared by sequential digestion with collagenase and trypsin. The isolation of the major glycopeptides was accomplished gel filtration ion exchange chromatography. glycohexapeptide, Gly-Met-Hyl (Gal-Glc)-Gly-His-Arg, has previously been characterized in digests various vertebrate collagens studied this other laboratories. Two known to be present human collagen, Gly-Phe-Hyl(Gal-Glc)-Gly-Ile-Arg Gly-Pro-Hyl(Gal) also isolated collagen. Three additional which had not reported purified their structures analyzed. them hexapeptides, Gly-Phe-Hyl(Gal)-Gly-Ile-Arg Gly-Pro-Hyl(Gal)-Gly-Glu-Leu, while a tripeptide, Gly-Met-Hyl(Gal). Characterization obtained α1 α2 components hexose analysis cyanogen bromide (CNBr) peptides derived whole as well both chains indicate presence only four sites glycosylation molecule. evidence presented is consistent existence an identical site each chain, corresponding disaccharide unit near NH2 terminus α1-CB5 peptide. two are located CNBr peptide α2-CB4 chain. There are, addition, minor limited number location all such same general area α suggest specific but unknown functional role synthesis, fibril formation, or basic aspects metabolism skin.