Isolation and partial characterization of the amino-terminal propeptide of type II procollagen from chick embryos

Publisher Website
Google Scholar
Abstract
The amino-terminal propeptide from type II procollagen was isolated from organ cultures of sternal cartilages from 17 day old chick embryos. The procedure provided the 1st isolation of the propeptide in amounts adequate for chemical characterization. The propeptide had an apparent MW of 18,000 as estimated by gel electrophoresis in sodium dodecylsulfate. It contained a collagen-like domain as demonstrated by its amino acid composition, circular dichroism spectrum and susceptibility to bacterial collagenase. One residue of hydroxylysine was present, the 1st time this amino acid was detected in a propeptide. The peptide contained no methionine and only 2 residues of half-cystine. Antibodies were prepared to the propeptide and were used to establish its identity. The antibodies precipitated type II procollagen but did not precipitate type II procollagen from which the amino and carboxy propeptides were removed with pepsin. They did not precipitate the carboxy propeptide of type II procollagen. The type II amino propeptide was similar to the amino propeptides of type I and type III procollagens in that it contained a collagen-like domain. It differed in that it lacked a globular domain of 77-86 residues found at the amino-terminal ends of the pro.alpha.1 chains of type I and type III procollagens.

This publication has 23 references indexed in Scilit: