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Partial characterization of type X collagen from bovine growth‐plate cartilage Evidence that type X collagen is processed in vivo
Author(s) -
Ayad Shirley,
Kwan Alvin P.L.,
Grant Michael E.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80899-2
Subject(s) - type ii collagen , in vivo , cartilage , type i collagen , chemistry , collagen, type i, alpha 1 , microbiology and biotechnology , biochemistry , anatomy , biology , endocrinology , extracellular matrix , genetics
Sequential extraction of bovine growth‐plate cartilage with 4 M guanidinium chloride and pepsin was used to identify the intact and pepsinized forms respectively of type X collagen. This collagen occurs predominantly as the processed [α 1 (X)] 3 form in vivo, although the procollagen [proα 1 (X)] 3 form can also be detected. The bovine proα 1 (X) and α 1 (X) chains have M r , values identical to the corresponding chick species ( M r 59 000 and 49 000). However, the pepsinized α 1 (X) p chains ( M r 47 000) are larger than those of the chick ( M r 45 000), and the bovine collagen type X is further distinguished by being disulphide‐bonded within the triple‐helical domain.