Isolation and partial characterization of bovine gingival AB collagen |
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Authors: | Mustafa Kh Dabbous Ola Hammouda Burcharda Brinkley |
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Institution: | (1) Departments of Biochemistry and Periodontics, Colleges of Medicine and Dentistry, University of Tennessee, Center for the Health Sciences, USA |
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Abstract: | 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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