Abstract

Analyses were performed to compare the (α1) 3 collagen molecule synthesized by the cartilaginous long bone anlage of 8-day chick embryos with that produced by adult cartilage, [α1(II)] 3. The embryonic molecule produced segment-long-spacing crystallites which had a banding pattern indistinguishable from that of authentic [α1(II)] 3. After carboxymethyl cellulose chromatography, the material in the α1 chain peak of the embryonic collagen was found to have the same amino acid composition as that of the α1(II) chain.

Full Text
Published version (Free)

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call