Open AccessPhysical Evidence for the Asembly of A and B Chains of Human Placental Collagen in a Single Triple Helix
Author(s) -
BENTZ Hanne,
BÄCHINGER Hans Peter,
GLANVILLE Robert,
KÜHN Klaus
Publication year - 1978
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1978.tb12778.x
Subject(s) - triple helix , collagen helix , molecule , chemistry , circular dichroism , crystallography , denaturation (fissile materials) , membrane , stereochemistry , biochemistry , organic chemistry , nuclear chemistry
Native collagen molecules containing A and B chains were isolated from pepsin‐solubilised human chorionic and amniotic membrane extracts by fractional salt precipitation and DEAE‐cellulose chromatography. They exhibited a circular dichroism spectrum, and a melting curve, characteristic for a triple‐helical structure. Electron microscopical investigations of their segment‐long‐spacing crystallites revealed a molecule similar to those of the interstitial types I, II and III collagens. After denaturation, the A and B chains were separated by DEAE‐cellulose chromatography and were consistently recovered in a ratio of 1:2. Renaturation experiments indicated that only the B chains are able to reform triple‐helical molecules which are stable under conditions in vivo . The data support a molecular formula A(B) 2 for the native collagen molecule.