Collagens from the skin and cartilage of the larval salamanderAmbystoma tigrinum

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Abstract
The major collagens of larval salamander (Ambystoma tigrinum) skin and cartilage were purified and characterized by CM‐cellulose chromatography and amino acid analysis of the component α chains. The collagens are similar to type I (skin) and type II (cartilage) collagens of birds and mammals. The type I molecule has the chain composition (α1)2α2, and the type II molecule is an (α1)3 molecule. Both collagens have lower levels of proline hydroxylation than the collagens isolated from homoiotherms, and generally higher serine contents. The type II collagen molecule has about half of its lysine residues hydroxylated, as in cartilage collagens of other species. Cyanogen bromide digestion of the component α chains followed by CM‐cellulose chromatography or SDS gel electrophoresis of the peptides confirms that each chain is a different gene product and allows identification of the collagens in this species. Similar collagens were isolated from newt (Notophthalmus viridescens) tissues by pepsin extraction and fractional salt precipitation. These data will allow more effective utilization of the regenerating salamander limb for studies of collagen metabolism during regeneration.