Lathyrism: aortic and cutaneous collagen in the rat.

In the rat the administration of lathyrogenic toxic agents at low doses over prolonged periods of time caused simultaneous alterations in aortic and cutaneous tissues. BAPN caused an increase in soluble collagen in the skin, but in aorta there was no increase in neutral salt soluble collagen, but an increase in the amount that could be solubilized with pepsin. Type III collagen was found to represent 7% in the control aorta samples and this level was not affected by BAPN.

The presence of type III collagen in the developing tooth.

Type I and type III collagens have been isolated from dental papilla and dental pulp of bovine tissues by enzymic digestion with pepsin and differential salt precipitation. Type III collagen was further purified by molecular sieve and ion-exchange chromatography. The relative proportions of type III and type I collagens were estimated by two different techniques, gel electrophoresis in the presence of mercaptoethanol, and direct estimation of the alpha1(III)CB3 peptide.

Changes in guinea-pig dermal collagen during development.

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.

Comparison of the cyanogen bromide peptides of insoluble guinea-pig skin and scar collagen.

Insoluble guinea-pig skin collagen and insoluble dermal scar collagen were cleaved with CNBr and the peptides derived from the alpha1-chain were separated by ion-exchange and molecular-sieve chromatography. Comparison of the peptides from scar collagen with those from skin collagen showed that the former contained more hydroxylysine. Separation of the CNBr peptides showed that this increase in hydroxylysine was found not only in the non-helical regions, but was also seen down the helical portion of the molecule.