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- W2054835887 abstract "Abstract Two forms of Achromobacter collagenase, A 1 and A 2 , of high molecular mass (110 and 90 kDa, respectively) were isolated from the supernatant of the culture of Vibrio alginolyticus chemovar iophagus . They have an identical C-terminal sequence, but different N-terminal sequences. They do not differ in specific activities toward synthetic substrate and collagen type I. In SDS-polyacrylamide electrophoresis gels containing copolymerized gelatine as substrate, bot A 1 and A 2 gave after autolysis similar active forms. It was deduced that A 1 differs from A 2 by a 20 kDa N-terminal fragment. The results obtained with their autodigestion and the incubation with EDTA indicate that each of them is composed of a single polypeptide chain containing several domains resistant to proteolysis. The purified IgG against pure 70 kDa Achromobacter collagenase used in our previous studies inhibited A 1 and A 2 activities. Similar inhibition curves were obtained for 70 kDa, 90 kDa and 110 kDa forms. All these data indicate that different active forms of Achromobacter collagenase are cleavage products derived from the same single polypeptide chain. A tentative model for an alignment of proteolytically resistant fragments and functional domains in A 1 polypeptide chain is proposed." @default.
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- W2054835887 date "1986-12-01" @default.
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- W2054835887 title "Purification and characterization of two high-molecular-mass forms of Achromobacter collagenase" @default.
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- W2054835887 doi "https://doi.org/10.1016/0167-4838(86)90028-2" @default.
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