Amino acid sequence and biological activities of another kunitz-type protease inhibitor isolated from the sea anemone Anthopleura aff. xanthogrammica

被引：7

作者：

Minagawa, S ^{[1
]}

Ishida, M ^{[1
]}

Shimakura, K ^{[1
]}

Nagashima, Y ^{[1
]}

Shiomi, K ^{[1
]}

机构：

[1] Tokyo Univ Fisheries, Dept Food Sci & Technol, Minato Ku, Tokyo 1088477, Japan

来源：

FISHERIES SCIENCE | 1998年 / 64卷 / 01期

关键词：

sea anemone; Anthopleura aff. xanthogrammica; serine protease inhibitor; Kunitz-type protease inhibitor; amino acid sequence;

D O I：

10.2331/fishsci.64.155

中图分类号：

S9 [水产、渔业];

学科分类号：

0908 ;

摘要：

In addition to the two protease inhibitors (AXPI-I and II) previously characterized, another inhibitor (AXPI-III) has been isolated from the aqueous extract of the sea anemone Anthopleura aff. xanthogrammica by acetone precipitation, gel filtration, cation-exchange FPLC, and reverse-phase HPLC. Like AXPI-I and II, AXPI-III is a basic polypeptide and its amino acid composition is characterized by the presence of 6 half-Cys residues and the absence of Met and Trp. AXPI-III is potently inhibitory against trypsin and also considerably inhibitory against alpha-chymotrypsin. Both AXPI-II and III did not inhibit the binding of I-125-alpha-dendrotoxin to rat synaptosomal membranes, suggesting that they are not blockers of voltage-sensitive potassium channels. Analyses of the N-terminal portion and one asparaginylendopeptidase-digested fragment established the complete amino acid sequence of AXPI-III comprising 61 residues. The overall sequence homology and the conserved location of half-Cys residues confirmed that AXPI-III belongs to the Kunitz-type family.

引用

页码：155 / 159

页数：5

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