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Burro aortic collagen: platelet aggregating activity and ultrastructural changes induced by plasma

Journal Article · · Am. J. Vet. Res.; (United States)
OSTI ID:6550219
 [1]; ;
  1. Comparative Animal Research Lab., Oak Ridge, TN
A fibrillar collagen molecule was extracted from the upper thoracic aorta of an old burro (Equus asinus). Presence of the collagen in the extract was determined by amino acid analysis, scanning and transmission electron microscopy, incubation with collagenase, and assays of its platelet-aggregating capacity by ''aggregometry.'' Based on the amino acid ratios of proline/hydroxyproline and lysine/hydroxylysine, the collagenous protein most nearly resembles type I of 4 main published types of collagen. Quantitative assays of the collagen as a mediator of platelet aggregation showed human platelets more sensitive and sheep platelets slightly less sensitive than burro platelets. Incubation with collagenase abolished platelet aggregation capacity and converted the fibrillar collagen to a gel-like mass. Incubation with galactose oxidase neither lessened nor intensified the collagen-mediated platelet aggregation. Incubation with burro plasma decreased platelet aggregating activity and changed the collagen ultrastructure (demonstrated with scanning electron microscopic imaging). The significance of a naturally occurring plasma (protein) factor(s) which may have a regulatory role in reducing the chemical activity of the fibrillar collagen molecule with platelets is also discussed.
OSTI ID:
6550219
Journal Information:
Am. J. Vet. Res.; (United States), Journal Name: Am. J. Vet. Res.; (United States) Vol. 39:3; ISSN AJVRA
Country of Publication:
United States
Language:
English