Maturation of collagenous tissue: Specific [formula omitted] proteolytic cleavage of only α1(I) chains

Abstract

A partially cleaved α1(I) chain, α1 χ, has been isolated from earlier synthesized or older (acid-extracted) guinea pig skin collagen. The α1 χ component is shown to be absent from the newly synthesized (neutral salt-extracted) collagen. This degradation is a result of specific in vivo proteolytic sission of α1(I) chain since the soluble collagen has no corresponding product from the α2 chain. The in vivo proteolytic cleavage is believed to result from processes related to natural physiological maturation of collagenous tissue.