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- W1581445717 abstract "Abstract Solutions of native Type III collagen (chain composition, [ α 1( III )] 3 ) exhibit a rapid and dramatic decrease in relative viscosity when incubated with trypsin. Cleavage products of the reaction were precipitated with ammonium sulfate and isolated in denatured form by molecular sieve chromatography. They were found to be comprised of: α1(III)-T1 (molecular weight, 71,000) derived from the NH 2 -terminal portion of the Type III molecule; and α1(III)-T2 (molecular weight, 24,000) from the COOH-terminal portion of the molecule. Determination of the amino acid sequence at the NH 2 -terminal portion of α1(III)-T2 as well as at the COOH-terminus of α(III)-T1 demonstrated that the products arose from specific cleavage of the type III molecule at an arginine-glycine bond corresponding to residues 780–781 in the repetitive triplet sequence of the α1(III) chain. The results suggest that the trypsin-susceptible bond in the native Type III collagen molecule resides in a region characterized by a relative lack of the normal collagen helicity." @default.
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- W1581445717 date "1976-04-01" @default.
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- W1581445717 title "Specific cleavage of the native Type III collagen molecule with trypsin" @default.
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- W1581445717 doi "https://doi.org/10.1016/0003-9861(76)90300-3" @default.
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