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 C18 reverse-phase HPLC. The molecular masses of RmIn I, RmIn II, and the complexes RmIn II/trypsin and RmIn I,II/α-chymotrypsin have been determined. The K i values of RmIn I and RmIn II for trypsin and α-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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Abbreviations
- BAPNA:
-
N-benzoyl-D,L-arginine p-nitroanilide
- BSA:
-
bovine serum albumin
- BTEE:
-
N-benzoyl-L-tyrosine ethyl ester
- HPLC:
-
high performance liquid chromatography
- TFA:
-
trifluoroacetic acid
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Original Russian Text © I. N. Sokotun, A. P. Il’ina, M. M. Monastyrnaya, E. V. Leychenko, A. A. Es’kov, S. D. Anastuk, E. P. Kozlovskaya, 2007, published in Biokhimiya, 2007, Vol. 72, No. 3, pp. 368–374.
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Sokotun, I.N., Il’ina, A.P., Monastyrnaya, M.M. et al. Proteinase inhibitors from the tropical sea anemone Radianthus macrodactylus: Isolation and characteristic. Biochemistry Moscow 72, 301–306 (2007). https://doi.org/10.1134/S0006297907030078
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DOI: https://doi.org/10.1134/S0006297907030078