作者: T.C. Blochberger , P.K. Cornuet , J.R. Hassell
DOI: 10.1016/S0021-9258(19)36731-6
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摘要: The proteoglycans extracted from adult chicken were initially purified by DEAE-chromatography. Digestion of these with chondroitinase ABC generated a single 40-kDa core protein while digestion keratanase 52-kDa protein. both enzymes combined, however, increased the amount produced. This suggested that exists chondroitin/dermatan sulfate (C/DS) side chains alone and C/DS keratan (KS) chains. proteoglycan fraction was digested ABC, M(r) = 40,000 derived containing isolated. Amino-terminal sequencing showed it to be chick cognate decorin. remaining then keratanase, proteins KS-containing purified. KS had same amino-terminal sequence as decorin cross-reacted antibodies Sequence lumican. results this study suggest corneas contain two isoforms decorin: one other, hybrid, Embryonic did not hybrid isoform These different post-translational modifications occur gene product during corneal development maturation.