Collagen polymorphism in mature rabbit cornea.
作者： I L Freeman
DOI:
关键词: Hydroxylysine 、 Gel electrophoresis 、 Lysine 、 Acetic acid 、 Biochemistry 、 Cornea 、 Carbohydrate 、 Peptide 、 Biology 、 Type I collagen 、 Molecular biology
摘要: Sequential extraction of mature rabbit corneal stroma with NaCl-Tris buffer and acetic acid solubilized only 12% the total collagen. Pepsin (E:S 1:10,4 degrees C, 48 hr) in 0.4 M 91% to 95% collagen residue. Approximately 68% material could be precipitated at 2.5M NaCl a further 3% 9% 3.5M NaCl. The collagenous precipitating contained alpha, beta, gamma, some higher molecular weight components had CNBr profile similar bovine type I skin It an hydroxylysine/lysine (OHLys/Lys) ratio 0.43, that collagen, but unlike was 52% glycosyled. Although precipitate peptide it two additional chains approximately 140,000 100,000 daltons, OHLys/Lys 0.62, 66% glycosylated. Individual were separated from precipitates by gel electrophoresis,and shown carbohydrate rich. These may derived one or more species which are physiologically important maintenance unique organization
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