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The hydrolysis of poly ( L ‐prolyl‐glycyl‐ L ‐prolyl) by bacterial collagenase
Author(s) -
Harper Elvin,
Berger Arieh,
Katchalski Ephraim
Publication year - 1972
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1972.360110807
Subject(s) - chemistry , collagenase , glycine , proline , hydrolysis , biochemistry , clostridium , substrate (aquarium) , enzyme , polymer , stereochemistry , bacteria , amino acid , organic chemistry , oceanography , biology , genetics , geology
Poly ( L ‐Prolyl‐Glycyl‐ L ‐Prolyl), a polymer which resembles collagen by physical and immunochemical criteria, has been shown to serve as a substrate for the highly specific bacterial collagenase obtained from Clostridium histolyticum . The postulated reaction products Gly Pro, Gly Pro Pro, and Pro Gly Pro Pro have been isolated. The enzyme has been employed as an analytical tool in elucidating the sequence of synthesized polymers of proline and glycine.

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