Purification and characterization of a peptide from the carboxy-terminal region of chick tendon procollagen type I.
作者： Bjorn R. Olsen , Norberto A. Guzman , Jurgen Engel , Chris Condit , Steinar Aase
DOI: 10.1021/BI00632A034
关键词: Procollagen peptidase 、 Carbohydrate 、 Trimer 、 Amino acid 、 Mannose 、 Chemistry 、 Stereochemistry 、 Anatomy 、 Peptide 、 Trypsin 、 Oligosaccharide
摘要: A disulfide-bonded peptide with a molecular weight of about 100 000 was isolated from the medium cultured chick embryo tendons. It shown to be trimer two types subunits in 2:1 ratio, and tryptic fingerprinting immunological evidence indicated that it derived carboxy-terminal-precursor-specific region procollagen. Amino acid analysis after reduction alkylation contains 30 residues half-cystine involved intrachain as well interchain disulfide bonding. The bonds could reduced alkylated under nondenaturing conditions. Carbohydrate showed each three chains N-acetylglucosamine ten mannose. This suggests presence one or oligosaccharide units per chain.
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