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dc.contributor.authorKielty, C
dc.contributor.authorHulmes, D
dc.contributor.authorSchor, Seth L
dc.contributor.authorGrant, M
dc.date.accessioned2011-03-08T16:22:07Z
dc.date.available2011-03-08T16:22:07Z
dc.date.issued1984-04-24
dc.identifier.citationEmbryonic chick cartilage collagens. Differences in the low-Mr species present in sternal cartilage and tibiotarsal articular cartilage. 1984, 169 (2):179-84 FEBS Letten
dc.identifier.issn0014-5793
dc.identifier.pmid6425083
dc.identifier.doi10.1016/0014-5793(84)80314-2
dc.identifier.urihttp://hdl.handle.net/10541/123966
dc.description.abstractThe 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, 1 alpha 2 alpha 3 alpha 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 (Mr 59 000), a major low-Mr procollagen-like species previously detected in chick chondrocyte cultures.
dc.language.isoenen
dc.subject.meshAmino Acids
dc.subject.meshAnimals
dc.subject.meshCartilage
dc.subject.meshCartilage, Articular
dc.subject.meshChick Embryo
dc.subject.meshCollagen
dc.subject.meshElectrophoresis, Polyacrylamide Gel
dc.subject.meshMicroscopy, Electron
dc.subject.meshMolecular Weight
dc.subject.meshPepsin A
dc.titleEmbryonic chick cartilage collagens. Differences in the low-Mr species present in sternal cartilage and tibiotarsal articular cartilage.en
dc.typeArticleen
dc.contributor.departmentDepartments of Biochemistry and Medical Biophysics, University of Manchester Medical School, Oxford Road, Manchester M13 9PTen
dc.identifier.journalFEBS Lettersen
html.description.abstractThe 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, 1 alpha 2 alpha 3 alpha 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 (Mr 59 000), a major low-Mr procollagen-like species previously detected in chick chondrocyte cultures.


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