Open AccessThe Properties of Molecular Fragments Obtained on Treating Calfskin Collagen with Collagenase from Clostridium histolyticum
Author(s) -
Stark M.,
Kühn K.
Publication year - 1968
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1968.tb00477.x
Subject(s) - collagenase , collagen helix , chemistry , triple helix , denaturation (fissile materials) , amino acid , molecule , molecular mass , peptide , cellulose , helix (gastropod) , crystallography , biochemistry , stereochemistry , biology , organic chemistry , nuclear chemistry , ecology , snail , enzyme
Collagenase was found to attack the collagen molecule at both ends at 10°. Six molecular fragments of different lengths were observed and could be correlated with the intact molecule as long‐spacing segment fragments. It was possible to isolate the 2,600,1,250 and 780 Å fragments by fractional ammonium sulphate precipitation. The sharp helix‐coil transition on denaturation shows that the fragments have an intact triple helix. It was possible to separate the two shorter fragments into three components (the α1, α2 and α3 chain fragments) by chromatography on CM cellulose. The α1 and α3 chains have very similar amino acid compositions and peptide maps for both these fragments. This suggests that the differences between these two components are probably due to telopeptides and not to the amino acid sequence of the main chain.