title: [Heterogeneity of collagen molecules types I and II according to their resistance to proteolysis].
abstract: 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.
authors.forename: B P
authors.initials: BP
authors.lastname: Sokolov
authors.forename: B M
authors.initials: BM
authors.lastname: Sher
authors.forename: E A
authors.initials: EA
authors.lastname: Kozlov
authors.forename: T A
authors.initials: TA
authors.lastname: Tsvetkova
authors.forename: A A
authors.initials: AA
authors.lastname: Del'vig
mesh_terms: 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
chemical_list: D003094:Collagen; D010434:Pepsin A
vernacular_title: Geterogennost' molekul kollagenov I i II tipov po ustoĭchivosti k proteolizu.