Heterogeneity of collagen molecules types i and Ii according to their resistance to proteolysis
Sokolov, B.P.; Sher, B.M.; Kozlov, E.A.; Tsvetkova, T.A.; Del'vig, A.A.
Biokhimiia 53(11): 1828-1836
1988
ISSN/ISBN: 0320-9725 PMID: 3150814 Document Number: 305872
Study of the effects of pepsin treatment on soluble collagens type I of the skin and collagens type II of the costal cartilage of healthy subjects revealed the presence of two classes of molecules differing in the stability of their three-helical structure. In collagen molecules possessing a low stability (their number may amount to 20-30%) within the temperature range of 4-30 degrees C pepsin causes a split-off of N-terminal sites with the formation of short chains, i.e., alpha 1(I), alpha 2(II), and alpha 1(II), whereas at higher temperatures (33 degrees C for collagens type I and 37 degrees C for collagens type II) a complete degradation of these molecules takes place. It was found that collagens types I and II molecules contain a high number of three-helical sites with a high susceptibility to pepsin. The putative functional role of structural heterogeneity of collagen molecules is discussed.