Sokotun I N, Il'ina A P, Monastyrnaya M M, Leychenko E V, Es'kov A A, Anastuk S D, Kozlovskaya E P
Pacific Institute of Bioorganic Chemistry, Far East Branch of the Russian Academy of Sciences, Vladivostok, Russia.
Biochemistry (Mosc). 2007 Mar;72(3):301-6. doi: 10.1134/s0006297907030078.
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.
已从热带海葵大指海葵中分离并鉴定出两种新的丝氨酸蛋白酶抑制剂（RmIn I和RmIn II）。纯化过程包括多色-1疏水色谱、Superdex Peptide 10/30快速蛋白质液相色谱以及Nucleosil C(18)反相高效液相色谱。已测定了RmIn I、RmIn II以及复合物RmIn II/胰蛋白酶和RmIn I,II/α-糜蛋白酶的分子量。已测定了RmIn I和RmIn II对胰蛋白酶和α-糜蛋白酶的抑制常数（K(i)值）。多肽RmIn I和RmIn II显示无毒且具有抗组胺活性。已测定了RmIn I（GICSEPIVVGPCKAG-）和RmIn II（GSTCLEPKVVGPCKA-）的N端氨基酸序列。结果表明，腔肠动物、爬行动物和哺乳动物等进化距离较远的物种所产生的蛋白酶抑制剂的氨基酸序列具有高度同源性。
