Further Characterization of Earthworm Serine Proteases: Cleavage Specificity Against Peptide Substrates and on Autolysis

Nobuyoshi Nakajima; Manabu Sugimoto; Kohji Ishihara; Kaoru Nakamura; Hiroki Hamada

doi:10.1271/bbb.63.2031

Further Characterization of Earthworm Serine Proteases: Cleavage Specificity Against Peptide Substrates and on Autolysis

Nobuyoshi Nakajima, Manabu Sugimoto, Kohji Ishihara, Kaoru Nakamura, Hiroki Hamada

Institute of Plant Science and Resources

Research output: Contribution to journal › Article › peer-review

33 Citations (Scopus)

Abstract

Cleavage specificity of two fibrinolytic enzymes from Lumbricus rubellus [Nakajima, N., et al., Biosci. Biotechnol. Biochem., 57, 1726-1730 (1993) and 60, 293-300 (1996)] was investigated using β-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.

Original language	English
Pages (from-to)	2031-2033
Number of pages	3
Journal	Bioscience, Biotechnology and Biochemistry
Volume	63
Issue number	11
DOIs	https://doi.org/10.1271/bbb.63.2031
Publication status	Published - Jan 1 1999

Keywords

Cleavage specificity
Earthworm
Fibrinolytic enzyme
Serine protease
β-amyloid

ASJC Scopus subject areas

Biotechnology
Analytical Chemistry
Biochemistry
Applied Microbiology and Biotechnology
Molecular Biology
Organic Chemistry

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title = "Further Characterization of Earthworm Serine Proteases: Cleavage Specificity Against Peptide Substrates and on Autolysis",

abstract = "Cleavage specificity of two fibrinolytic enzymes from Lumbricus rubellus [Nakajima, N., et al., Biosci. Biotechnol. Biochem., 57, 1726-1730 (1993) and 60, 293-300 (1996)] was investigated using β-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.",

keywords = "Cleavage specificity, Earthworm, Fibrinolytic enzyme, Serine protease, β-amyloid",

author = "Nobuyoshi Nakajima and Manabu Sugimoto and Kohji Ishihara and Kaoru Nakamura and Hiroki Hamada",

year = "1999",

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doi = "10.1271/bbb.63.2031",

language = "English",

volume = "63",

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T1 - Further Characterization of Earthworm Serine Proteases

T2 - Cleavage Specificity Against Peptide Substrates and on Autolysis

AU - Nakajima, Nobuyoshi

AU - Sugimoto, Manabu

AU - Ishihara, Kohji

AU - Nakamura, Kaoru

AU - Hamada, Hiroki

PY - 1999/1/1

Y1 - 1999/1/1

N2 - Cleavage specificity of two fibrinolytic enzymes from Lumbricus rubellus [Nakajima, N., et al., Biosci. Biotechnol. Biochem., 57, 1726-1730 (1993) and 60, 293-300 (1996)] was investigated using β-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.

AB - Cleavage specificity of two fibrinolytic enzymes from Lumbricus rubellus [Nakajima, N., et al., Biosci. Biotechnol. Biochem., 57, 1726-1730 (1993) and 60, 293-300 (1996)] was investigated using β-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.

KW - Cleavage specificity

KW - Earthworm

KW - Fibrinolytic enzyme

KW - Serine protease

KW - β-amyloid

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SN - 0916-8451

VL - 63

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JO - Bioscience, Biotechnology and Biochemistry

JF - Bioscience, Biotechnology and Biochemistry

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ER -

Further Characterization of Earthworm Serine Proteases: Cleavage Specificity Against Peptide Substrates and on Autolysis

Abstract

Keywords

ASJC Scopus subject areas

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