Analysis of the reducible components of the muscle protein, connectin: absence of lysine-derived cross-links

After exhaustive salt extractions of rabbit and human skeletal muscle, the amino acid compositions of the residual proteins were similar to those reported for connectin. Complete removal of collagen contamination was achieved only after treatment of the connectin preparations with bacterial collagenase. On reduction with KB³H₄, the small amounts of lysine-derived reducible cross-links that were present in the initial connectin preparations were completely absent after treatment with collagenase. In adult human connectin some hexitol-lysine derivatives were present after reduction. These results indicate that, in contrast to previous reports, connectin does not participate in the same lysyl oxidase-mediated cross-linking system that occurs in collagen and elastin.