Further characterization of earthworm serine proteases: Cleavage specificity against peptide substrates and on autolysis

被引：32

作者：

Nakajima, N ^{[1
]}

Sugimoto, M

Ishihara, K

Nakamura, K

Hamada, H

机构：

[1] Okayama Prefectural Univ, Dept Nutr Sci, Okayama 7191112, Japan

[2] Okayama Univ, Bioresources Res Inst, Kurashiki, Okayama 7100046, Japan

[3] Kyoto Univ Educ, Dept Chem, Fushimi Ku, Kyoto 6128522, Japan

[4] Kyoto Univ, Chem Res Inst, Kyoto 6110011, Japan

[5] Okayama Univ Sci, Dept Appl Sci, Okayama 7000005, Japan

来源：

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 1999年 / 63卷 / 11期

关键词：

serine protease; earthworm; cleavage specificity; beta-amyloid; fibrinolytic enzyme;

D O I：

10.1271/bbb.63.2031

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Cleavage specificity of two fibrinolytic enzymes from Lumbricus rubellus [Nakajima, N., ct al., Biosci. Biotechnol. Biochem., 57, 1726-1730 (1993) and 60, 293-300 (1996)] was investigated using beta-amyloid 1-40 and oxidized insulin B-chain as peptide substrates. The serine protease, F-III-2, cleaved the former substrate at six sites, and the latter at five sites. F-II digested them at six and ten, respectively. The cleavage specificity of F-III-2 resembled those of both trypsin and chymotrypsin. F-II had a broader specificity than F-III-2 and preferred also the bonds consisting neutral or hydrophobic amino acids. Furthermore, F-III-2 itself was digested initially on the site of Arg(144)-Tyr(145) to produce two peptide fragments, when it was autolyzed regularly by heating.

引用

页码：2031 / 2033

页数：3

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