Abstract
1.1. Collagen from the newt, Triturus viridescens, has been characterized according to amino acid composition, melting temperature, migration of components on disc gel electrophoresis and formation of native and sement long spacing fibers in vitro.2.2. Collagens extracted both by acetic acid alone and acetic acid plus pepsin, were similar, though differences in electrophoretic migration and amino acid composition were noted.3.3. Newt collagen was similar to previously reported vertebrate species.4.4. Observed differences, in the distribution of hydroxy amino acids in newt collagen,were reflected by the melting tempeture.
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