Open AccessChanges in Guinea‐Pig Dermal Collagen during Development
Author(s) -
SHUTTLEWORTH C. Adrian,
FORREST Leslie
Publication year - 1975
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1975.tb02174.x
Subject(s) - guinea pig , chemistry , pepsin , dermis , collagen, type i, alpha 1 , proline , type i collagen , biochemistry , fetus , amino acid , microbiology and biotechnology , enzyme , biology , endocrinology , anatomy , extracellular matrix , genetics , pregnancy
Guinea‐pig dermis was digested with pepsin and the solubilized collagen molecules separated by differential salt precipitation at pH 7.5. Differences in subunit composition and amino acid analysis were noted between type I and type III collagen. Incorporation of radioactive proline into the developing foetus enabled isolation of labelled type I and type III collagens. Comparison of the specific activity of the isolated collagen molecules showed that type III collagen had a high specific activity in the early stages of foetal development, which decreased dramatically during foetal development. The specific activity of pepsin‐solubilized type I collagen remained fairly constant during foetal development.