Isoforms of corneal keratan sulfate proteoglycan.
作者： J L Funderburgh , G W Conrad
DOI: 10.1016/S0021-9258(19)39071-4
关键词:
摘要: Bovine corneal keratan sulfate proteoglycan was found to contain three major protein components. Two proteins (37 and 25 kDa) were released from the by endo-beta-galactosidase, N-glycanase, or chemical deglycosylation. A smaller (20 kDa), not covalently linked sulfate, co-purified with conventional high performance ion exchange chromatography, ethanol precipitation, affinity purification on columns of monoclonal antibody but could be separated gel filtration chromatography in dissociative agents. The produced different fragmentation patterns sodium dodecyl sulfate-polyacrylamide electrophoresis after digestion V8 protease, each had unique two-dimensional tryptic peptide maps. N-terminal amino acid sequence core differed. In addition, proteoglycans containing these differed molecular size, suggesting levels glycosylation two proteins. Similarity suggested similar composition, similarities maps, antigenic cross-reactivity. Corneal proteoglycan, therefore, seems occur different, related, forms whose may represent members a homologous family.
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