Proteinase inhibitors from the tropical sea anemone Radianthus macrodactylus: Isolation and characteristic |
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Authors: | I. N. Sokotun A. P. Il’ina M. M. Monastyrnaya E. V. Leychenko A. A. Es’kov S. D. Anastuk E. P. Kozlovskaya |
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Affiliation: | (1) Pacific Institute of Bioorganic Chemistry, Far East Branch of the Russian Academy of Sciences, pr. 100-let Vladivostoku 159, 690022 Vladivostok, Russia |
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Abstract: | Two new serine proteinase inhibitors (RmIn I and RmIn II) from the tropical sea anemone Radianthus macrodactylus have been isolated and characterized. The purification procedure includes polychrome-1 hydrophobic chromatography, Superdex Peptide 10/30 FPLC, and Nucleosil C(18) reverse-phase HPLC. The molecular masses of RmIn I, RmIn II, and the complexes RmIn II/trypsin and RmIn I,II/alpha-chymotrypsin have been determined. The K(i) values of RmIn I and RmIn II for trypsin and alpha-chymotrypsin have been determined. The polypeptides RmIn I and RmIn II are shown to be nontoxic and to exhibit antihistamine activity. The N-terminal amino acid sequences of RmIn I (GICSEPIVVGPCKAG-) and RmIn II (GSTCLEPKVVGPCKA-) have been determined. A high homology of the amino acid sequences is demonstrated for the proteinase inhibitors produced by such evolutionarily distant species as coelenterates, reptiles, and mammals. |
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Keywords: | sea anemone serine proteinase inhibitor trypsin chymotrypsin inhibition constant amino acid sequence |
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