Abstract
1. 1. The origin of the various muscle phosphagens during evolution is considered in the context of the need to conserve ornithine for the synthesis of proline for connective tissue necessary for structural strength and flexibility and/or a complicated musculature. In each phosphagen, arginine is known to have contributed its amidine moiety thus maintaining the function of the phosphagen and setting free the proline precursor ornithine. 2. 2. Tissues from an earthworm, a starfish and a sea-squirt have been found to contain the enzymes arginase, ornithine aminotransferase and pyrroline-5-carboxylate reductase which are necessary to convert arginine to proline. 3. 3. For each of the animals studied analysis for the relevant free amino acids and for the characteristic amino acids (Pro, Oh-Pro, Oh-Lys, Gly) of collagen are presented. 4. 4. The amino acid composition of the diet of the sea-squirt Pyura stolonifera and of the starfish Coscinasterias calamaria is presented along with the level of the phosphagen kinases of the animals studied. 5. 5. The significance of the experimental results is discussed in connection with the importance of the transamidination reaction.
Published Version
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