作者: W G Cole , D Chan , A J Hickey , D E L Wilcken
DOI: 10.1042/BJ2190451
关键词: Peptide 、 Chemistry 、 Type I collagen 、 Collagen, type I, alpha 1 、 Glycosaminoglycan 、 Guanidinium chloride 、 Pepsin 、 Dermis 、 Biochemistry 、 Hydroxylysine
摘要: The collagens were studied in 13 normal and 19 myxomatous human mitral valves. of the valve completely solubilized by using a method consisting guanidinium chloride extraction, limited pepsin digestions CNBr cleavage residue. valves contained 74% type I, 24% III 2% V collagen. I had similar solubility patterns, although only collagen was detected extract. Type first higher contents hydroxylysine than did same from age-matched dermis. two-dimensional electrophoretic ‘maps’ CNBr-cleavage peptides showed low recoveries C-terminal alpha 1(I) CB6 1(III) CB9 peptides, which are involved forming intermolecular cross-linkages. Most reducible cross-linkages present large-Mr peptide complexes, these complexes shown labelling with 125I to include tyrosine-containing peptide. 67% 31% collagens. There significant increase concentration each collagen, consisted 9% 53% 25% not differ significantly results obtained biochemical findings suggest that there is an increased production particular glycosaminoglycan as well proliferation cells part repair process