ウメボシイソギンチャクのセリンプロテア-ゼインヒビタ-の単離および性状〔英文〕

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Four serine protease inhibitors (AEPI-I, II, III and IV) were isolated from the sea anemone Actinia equina by acetone precipitation, gel filtration, ion-exchange HPLC and reversed-phase HPLC. They were all basic polypeptides with a molecular weight ranging from 6200 to 7000. The amino acid compositions of the inhibitors were very close to one another; they were characterized by the presence of 6 half-cystinyl residues but the absence of methionine and tryptophan. The inhibitors were active against serine proteases; inhibition for trypsin and α-chymotrypsin was displayed by the four inhibitors while that for kallikrein only by AEPI-I and II and that for plasmin only by AEPI-III and IV. However, none of the inhibitors showed affinity for both metalloproteases and cysteine proteases. These results suggested that the protease inhibitors can be classified into Kunitz-type inhibitors.
日本水産學會の論文