Open AccessRenaturation of disulfide‐linked procollagen
Author(s) -
Fessler Liselotte I.,
Rudd Colette,
Fessler John H.
Publication year - 1974
Publication title -
journal of supramolecular structure
Language(s) - English
Resource type - Journals
eISSN - 1547-9366
pISSN - 0091-7419
DOI - 10.1002/jss.400020205
Subject(s) - procollagen peptidase , disulfide bond , chemistry , intramolecular force , pepsin , biochemistry , molecule , stereochemistry , biology , microbiology and biotechnology , enzyme , organic chemistry
Disulfide‐linked, triple‐stranded procollagen (pro γ 112) was isolated from chick embryo skull bones. It was reversibly denatured and renatured as judged by sedimentation properties and susceptibility to digestion with pepsin. Refolding was an intramolecular process and aggregation between molecules did not occur.