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In vitro blood compatibility of glycosaminoglycan-precipitated collagens

✍ Scribed by Silver, F. H. ;Yannas, I. V. ;Salzman, E. W.

Publisher
John Wiley and Sons
Year
1979
Tongue
English
Weight
799 KB
Volume
13
Category
Article
ISSN
0021-9304

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✦ Synopsis

Abstract

Precipitation of bovine hide collagen by chondroitin 6‐sulfate at low __p__H and subsequent crosslinking enhances the blood compatibility of native collagen. Both dehydrothermal crosslinking and complexation with chondroitin 6‐sulfate separately decrease the platelet‐aggregating activity of collagen. Crosslinking also decreases the number of free acidic and free basic residues on collagen, which suggests that crosslinking involves these residues in condensation reactions with formation of intrachain and interchain synthetic peptide bonds. Clotting times for collagen precipitated with chondroitin 6‐sulfate indicate the this surface does not activate or interfere with coagulation via either the intrinsic or extrinsic pathway. These findings support further consideration of collagen modified by chondroitin 6‐sulfate as a blood compatible material.

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