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Embryonic chick cartilage collagens
Author(s) -
Kielty C.M.,
Hulmes D.J.S.,
Schor S.L.,
Grant M.E.
Publication year - 1984
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(84)80314-2
Subject(s) - cartilage , embryonic stem cell , microbiology and biotechnology , chemistry , anatomy , biology , biochemistry , gene
The collagenous polypeptides present in embryonic chick sternal and tibiotarsal cartilages have been solubilised by digestion with pepsin and separated by salt fractionation. Type II collagen, 1α2α3α collagen, and two polypeptides (apparent molecular mass 150 and 42 kDa), which were reducible to a number of smaller peptides, were extracted from both tissues. However, also present in the peptic digests of tibiotarsal cartilages was a major non‐reducible highly‐soluble polypeptide of 45 kDa. This short‐chain collagen is apparently identical to the pepsinized product of G collagen ( M r 59 000), a major low‐ M r procollagen‐like species previously detected in chick chondrocyte cultures.