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Identification of disulphide‐bonded type X procollagen polypeptides in embryonic chick chondrocyte culture
Author(s) -
Kwan A.P.L.,
Sear C.H.J.,
Grant M.E.
Publication year - 1986
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(86)80994-2
Subject(s) - procollagen peptidase , chemistry , dimer , chondrocyte , embryonic stem cell , peptide , cartilage , molecular mass , biochemistry , microbiology and biotechnology , biology , anatomy , gene , enzyme , in vitro , organic chemistry
A high‐ M r ( M r 120000), disulphide‐bonded collagenous polypeptide was observed to co‐purify with the proα 1 (X) chain during isolation of cartilage collagens from culture medium of embryonic chick tibiotarsal chondrocytes. This high‐ M r polypeptide was subsequently shown by two‐dimensional SDS‐PAGE and peptide mapping to represent a dimer of the proα 1 (X) chain of type X collagen linked by disulphide bonding in the non‐collagenous domains.