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

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

29 Citations (Scopus)

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.

Original language	English
Pages (from-to)	254-262
Number of pages	9
Journal	Protein Expression and Purification
Volume	36
Issue number	2
DOIs	https://doi.org/10.1016/j.pep.2004.05.001
Publication status	Published - Aug 2004
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biotechnology

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This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.pep.2004.05.001

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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.",

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. ",

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language = "English",

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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.

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

Abstract

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