Determination of the complete cDNA sequence, construction of expression systems, and elucidation of fibrinolytic activity for Tapes japonica lysozyme

Kouhei Takeshita; Yoshio Hashimoto; Yoshiyuki Thujihata; Takanori So; Tadashi Ueda; Taiji Iomoto

doi:10.1016/j.pep.2004.05.001

Determination of the complete cDNA sequence, construction of expression systems, and elucidation of fibrinolytic activity for Tapes japonica lysozyme

Kouhei Takeshita, Yoshio Hashimoto, Yoshiyuki Thujihata, Takanori So, Tadashi Ueda, Taiji Iomoto^*

^*この論文の責任著者

分子細胞機能学研究室

研究成果: ジャーナルへの寄稿 › 学術論文 › 査読

30 被引用数 (Scopus)

抄録

The lysozyme of the marine bivalve, Tapes japonica (13.8kDa), belongs to the invertebrate lysozyme family and displays both chitinase and isopeptidase activities. We determined the complete cDNA sequence and constructed effective expression systems for this enzyme using Escherichia coli (BL21) and Pichia pastoris. The native and recombinant proteins indicated lysozyme activity and isopeptidase activity, including the proteolysis of D-dimer, a plasminolytic product of stabilized polymeric fibrin. These results will be utilized for the structural and functional study of invertebrate lysozymes, and for the development of applications for thrombosis therapies.

本文言語	英語
ページ（範囲）	254-262
ページ数	9
ジャーナル	Protein Expression and Purification
巻	36
号	2
DOI	https://doi.org/10.1016/j.pep.2004.05.001
出版ステータス	出版済み - 2004/08

ASJC Scopus 主題領域

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10.1016/j.pep.2004.05.001

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引用スタイル

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title = "Determination of the complete cDNA sequence, construction of expression systems, and elucidation of fibrinolytic activity for Tapes japonica lysozyme",

abstract = "The lysozyme of the marine bivalve, Tapes japonica (13.8kDa), belongs to the invertebrate lysozyme family and displays both chitinase and isopeptidase activities. We determined the complete cDNA sequence and constructed effective expression systems for this enzyme using Escherichia coli (BL21) and Pichia pastoris. The native and recombinant proteins indicated lysozyme activity and isopeptidase activity, including the proteolysis of D-dimer, a plasminolytic product of stabilized polymeric fibrin. These results will be utilized for the structural and functional study of invertebrate lysozymes, and for the development of applications for thrombosis therapies.",

keywords = "Bi-functional, Expression, Fibrinolytic, Folding, Invertebrate type lysozyme",

author = "Kouhei Takeshita and Yoshio Hashimoto and Yoshiyuki Thujihata and Takanori So and Tadashi Ueda and Taiji Iomoto",

note = "Funding Information: This work was supported in part by grants from the Japan Foundation for Applied Enzymology and from the Foundation for Advanced Medicine (Japan). The authors thank KN-International (USA) for improvement of our English. ",

year = "2004",

month = aug,

doi = "10.1016/j.pep.2004.05.001",

language = "英語",

volume = "36",

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journal = "Protein Expression and Purification",

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publisher = "Academic Press Inc.",

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TY - JOUR

T1 - Determination of the complete cDNA sequence, construction of expression systems, and elucidation of fibrinolytic activity for Tapes japonica lysozyme

AU - Takeshita, Kouhei

AU - Hashimoto, Yoshio

AU - Thujihata, Yoshiyuki

AU - So, Takanori

AU - Ueda, Tadashi

AU - Iomoto, Taiji

N1 - Funding Information: This work was supported in part by grants from the Japan Foundation for Applied Enzymology and from the Foundation for Advanced Medicine (Japan). The authors thank KN-International (USA) for improvement of our English.

PY - 2004/8

Y1 - 2004/8

N2 - The lysozyme of the marine bivalve, Tapes japonica (13.8kDa), belongs to the invertebrate lysozyme family and displays both chitinase and isopeptidase activities. We determined the complete cDNA sequence and constructed effective expression systems for this enzyme using Escherichia coli (BL21) and Pichia pastoris. The native and recombinant proteins indicated lysozyme activity and isopeptidase activity, including the proteolysis of D-dimer, a plasminolytic product of stabilized polymeric fibrin. These results will be utilized for the structural and functional study of invertebrate lysozymes, and for the development of applications for thrombosis therapies.

AB - The lysozyme of the marine bivalve, Tapes japonica (13.8kDa), belongs to the invertebrate lysozyme family and displays both chitinase and isopeptidase activities. We determined the complete cDNA sequence and constructed effective expression systems for this enzyme using Escherichia coli (BL21) and Pichia pastoris. The native and recombinant proteins indicated lysozyme activity and isopeptidase activity, including the proteolysis of D-dimer, a plasminolytic product of stabilized polymeric fibrin. These results will be utilized for the structural and functional study of invertebrate lysozymes, and for the development of applications for thrombosis therapies.

KW - Bi-functional

KW - Expression

KW - Fibrinolytic

KW - Folding

KW - Invertebrate type lysozyme

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U2 - 10.1016/j.pep.2004.05.001

DO - 10.1016/j.pep.2004.05.001

M3 - 学術論文

C2 - 15249048

AN - SCOPUS:3142643627

SN - 1046-5928

VL - 36

SP - 254

EP - 262

JO - Protein Expression and Purification

JF - Protein Expression and Purification

IS - 2

ER -