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Collagen Cross‐Linking and Resorption: Effect of Glutaraldehyde Concentration
Author(s) -
Roe Simon C.,
Milthorpe Bruce K.,
Schindhelm Klaus
Publication year - 1990
Publication title -
artificial organs
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.684
H-Index - 76
eISSN - 1525-1594
pISSN - 0160-564X
DOI - 10.1111/j.1525-1594.1990.tb03001.x
Subject(s) - glutaraldehyde , collagenase , resorption , chemistry , in vivo , implant , biomaterial , tendon , in vitro , biomedical engineering , biochemistry , chromatography , surgery , enzyme , endocrinology , biology , medicine , microbiology and biotechnology , organic chemistry
Cross‐linked collagen bioprostheses usually are designed to be inert and nonresorbable, resulting in fatigue and wear failure in high‐stress environments. Eventual replacement of the implant, although minimizing strength loss during resorption, would result in a graft with reparative ability. Kangaroo tail tendon (KTT) partially cross‐linked with glutaraldehyde (GA) was evaluated in vitro for resistance to bacterial collagenase digestion and in vivo for biocompatibility and resorbability in an intramuscular implant assay. Cross‐linking was quantified by thermal denaturation studies. Incomplete cross‐linking was achieved with concentrations of GA >0.1% (w/v). KTT cross‐linked in <=0.05% GA were collagenase resistant being incompletely digested after 240 h. Cross‐linking of KTT with low concentrations of GA resulted in partial collagenase resistance and slowed resorption.