<b>PARTIAL PURIFICATION AND CHARACTERIZATION OF PROTEODERMATAN SULPHATE-DEGRADING PROTEINASES PRODUCED BY HUMAN GINGIVAL </b><b>FIBROBLASTS </b>

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<p>Two enzymes capable of degrading the protein core of proteodermatan sulphate were isolated and partially purified in latent form from medium conditioned by the culture of fibroblasts from human gingiva. One of these enzymes had a pH optimum of close to 7 and the other of close to 6. The molecular weight of the latent ‘neutral’ proteinase, determined by gel-filtration chromatography, was 48,000, decreasing to 37,000 and 19,000 on activation by limited proteolysis with trypsin. For the ‘acidic’ proteinase the molecular weights for latent and active forms were 68,000 and 57,000, respectively. Both enzymes were inhibited by ethylene-diaminetetra-acetic acid and by 1,10-phenanthroline but not by N-ethylmaleimide, phenylmethanesulphonyl fluoride, leupeptin or pepstatin. They are therefore probably metalloproteinases. Limited digestion of proteodermatan sulphate with either enzyme yielded a large fragment including about 200 amino acids from the aminoterminus and the dermatan sulphate chain, together with a number of smaller fragments derived from the C-terminal portion of the core. Prolonged digestion resulted in conversion of the large fragment to small peptides.</p>

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  • Biomedical Research

    Biomedical Research 9 (4), 269-279, 1988

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