Structural Property of Decorin from Small Intestine and its Effect of Type I Collagen Fibril Formation

Decorin was isolated from 4M guanidine HCl extracts of small intestine by ion exchange chromatography and cesium chloride density ultracentrifugation.Decorin and its core protein showed a broad band at about 110kDa and a narrow single band at 45kDa, respectively by SDS-PAGE.Anti-decorin core protein antiserum from pig skin corium reacted with the both decorin and its core protein from small intestine as judged by ELISA and immunoblotting.Peptide mapping pattern and NH2-terminal amino acid sequence of core protein from small intestine were not different from that of core protein from skin corium.Glycosaminoglycan of small intestine decorin was identified as dermatan sulfate by electrophoresis on cellulose-acetate membrane and chondroitinase-digestivity.Decorin accelerated type I collagen fibril formation, and reduced the gel strength of reconstructed collagen fibril.Anim.Sci.Technol.(Jpn.)69 ( 8)