All three chains of 1 alpha 2 alpha 3 alpha collagen from hyaline cartilage resist human collagenase.
A previous report that the 3 alpha collagen chain of hyaline cartilage was cleaved by human collagenase could not be confirmed when the 1 alpha 2 alpha 3 alpha collagen fraction was freed of all contaminating type II collagen. All three minor collagen chains, 1 alpha, 2 alpha and 3 alpha, were totally resistant to highly purified collagenases from both rheumatoid synovial and gastric mucosal tissues. This finding and CNBr-peptide patterns suggest that, despite the close homology with alpha 1 (II), the 3 alpha chain is a unique collagen component, possibly combined with 1 alpha and 2 alpha in heterotrimeric molecules. In contrast, a 3 alpha-like component from fibrocartilage was cleaved by collagenase and gave a CNBr-peptide pattern more typical of alpha 1 (II) than of the collagenase-resistant 3 alpha of hyaline cartilage.
D000818:Animals; D002358:Cartilage, Articular / Q000032:analysis*; D002417:Cattle; D003094:Collagen / Q000302:isolation & purification; D003488:Cyanogen Bromide; D004591:Electrophoresis, Polyacrylamide Gel; D005753:Gastric Mucosa / Q000201:enzymology; D006801:Humans; D046911:Macromolecular Substances; D008297:Male; D003012:Microbial Collagenase / Q000494:pharmacology*; D010446:Peptide Fragments / Q000302:isolation & purification; D013582:Synovial Fluid / Q000201:enzymology
D046911:Macromolecular Substances; D010446:Peptide Fragments; D003094:Collagen; D003012:Microbial Collagenase; D003488:Cyanogen Bromide