[Heterogeneity of collagen molecules types I and II according to their resistance to proteolysis].
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.
Sokolov
B P
BP
Sher
B M
BM
Kozlov
E A
EA
Tsvetkova
T A
TA
Del'vig
A A
AA
D002356:Cartilage / Q000032:analysis; D003094:Collagen / Q000032:analysis*; D006868:Hydrolysis; D010434:Pepsin A / Q000378:metabolism*; D011487:Protein Conformation; D011489:Protein Denaturation; D012867:Skin / Q000032:analysis; D013696:Temperature
D003094:Collagen; D010434:Pepsin A
Geterogennost' molekul kollagenov I i II tipov po ustoĭchivosti k proteolizu.