Summary
Limited proteolysis with pepsin solubilized 25% of the insoluble gingival matrix as mainly soluble collagenous material. Fractional salt precipication at neutral pH resulted in the separation of types III and I at 1.8 and 2.6 M NaCl, respectively. In addition, a collagenous fraction accounting for 2% of the solubilized collagen and precipitating at 4.5 M NaCl was shown to be identical with type V collagen. Isolation and partial characterization of the constituent-α-chains of the 4.5 M PPT by gel filtration, ion exchange and hydroxylapatite chromatography as well as disc electrophoresis showed that gingival type V collagen contains αA and αB chains in a ratio αB/αA of 1.73–1.8. Electron microscopic examination of ATP-precipitates showed that this collagen type gave only one kind of SLS aggregates with asymmetric band pattern characteristically different from that of type I collagen. The data provide evidence that gingival AB collagen is a heteropolymer in which the αA and αB chains are assembled in the same macromolecule in a 1∶2 ratio.
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Dabbous, M.K., Hammouda, O. & Brinkley, B. Isolation and partial characterization of bovine gingival AB collagen. Mol Cell Biochem 34, 87–93 (1981). https://doi.org/10.1007/BF02354862
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DOI: https://doi.org/10.1007/BF02354862