Van der Rest M, Rosenberg L C, Olsen B R, Poole A R
Biochem J. 1986 Aug 1;237(3):923-5. doi: 10.1042/bj2370923.
The primary structure of the cartilage matrix molecule chondrocalcin has been found to be identical with that of the C-propeptide of type II procollagen by comparing sequence analyses of the N-terminal regions and of tryptic peptides derived from chondrocalcin. This implies that in type II collagen the C-propeptide of type II collagen is employed not only in the assembly of the triple helix of type II collagen, as demonstrated previously, but in calcifying cartilage it may also be involved in those events leading to cartilage calcification, as earlier indicated.
通过比较软骨钙素N端区域和源自软骨钙素的胰蛋白酶肽段的序列分析,发现软骨基质分子软骨钙素的一级结构与II型前胶原的C-前肽相同。这意味着在II型胶原中,II型胶原的C-前肽不仅如先前所示参与II型胶原三螺旋的组装,而且在钙化软骨中,它也可能如早期所指出的那样参与导致软骨钙化的那些过程。