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Further biochemical and physicochemical characterization of minor disulfide‐bonded (type IX) collagen, extracted from foetal calf cartilage
Author(s) -
RicardBlum Sylvie,
Tiollier Jérôme,
Garrone Robert,
Herbage Daniel
Publication year - 1985
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.240270405
Subject(s) - pepsin , hydroxyproline , chemistry , cleavage (geology) , cartilage , differential scanning calorimetry , disulfide bond , molecule , type ii collagen , proline , crystallography , biochemistry , biophysics , stereochemistry , enzyme , anatomy , organic chemistry , materials science , amino acid , biology , physics , fracture (geology) , composite material , thermodynamics
Minor disulfide‐bonded collagen (previously termed X 1 –X 7 and now called type IX collagen) was isolated from foetal calf cartilage after pepsin treatment. At least three native fractions, containing, respectively, the X 1 X 2 X 3 , X 4 , and X 5 X 6 X 7 chains, were separated; and from further biochemical and physicochemical experiments (differential scanning calorimetry, electrical birefringence, rotary shadowing), we propose a tentative model for their organization within a parent molecule, X 1 and X 2 are molecules composed of three chains of apparent M r 62,000 and 50,000 linked by interchain disulfide bonds and containing pepsin‐sensitive regions. The cleavage of at least three of these sites, present within X 2 , gives rise to the X 3 and X 5 X 6 X 7 fractions composed of molecules 80–100 nm and 40–55 nm in length, respectively. The X 5 X 6 X 7 fraction is not digested by pepsin at 30°C owing to its high thermal stability (certainly explained by its high hydroxyproline + proline content). This organization is in good accordance with that proposed for chicken cartilage type IX collagen; differences could only exist in the number and (or) the location of the pepsin‐sensitive sites.