cDNA cloning and expression of mutant catalase from the hypocatalasemic mouse: Comparison with the acatalasemic mutant

Da Hong Wang; Ken Tsutsui; Kuniaki Sano; Noriyoshi Masuoka; Shohei Kira

doi:10.1016/S0167-4781(01)00316-5

cDNA cloning and expression of mutant catalase from the hypocatalasemic mouse: Comparison with the acatalasemic mutant

Da Hong Wang, Ken Tsutsui, Kuniaki Sano, Noriyoshi Masuoka, Shohei Kira

Graduate School of Medicine Dentistry and Pharmaceutical Sciences

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

22 Citations (Scopus)

Abstract

Mutant catalase cDNAs from the hypocatalasemic and acatalasemic mice were cloned and expressed in bacteria. A novel missense mutation, Asp (AAT) to Ser (AGT), was identified at amino acid position 439 of the hypocatalasemic catalase. Analysis of recombinant catalase mutants revealed that the mutation is responsible for the reduced activity of hypocatalasemic catalase and the unstable tetrameric structure of acatalasemic catalase was also suggested.

Original language	English
Pages (from-to)	217-220
Number of pages	4
Journal	Biochimica et Biophysica Acta - Gene Structure and Expression
Volume	1522
Issue number	3
DOIs	https://doi.org/10.1016/S0167-4781(01)00316-5
Publication status	Published - Dec 30 2001

Keywords

Acatalasemic mouse
Catalase
Hypocatalasemic mouse
cDNA cloning
cDNA expression

ASJC Scopus subject areas

Structural Biology
Biophysics
Biochemistry
Genetics

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10.1016/S0167-4781(01)00316-5

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cDNA cloning and expression of mutant catalase from the hypocatalasemic mouse : Comparison with the acatalasemic mutant. / Wang, Da Hong; Tsutsui, Ken; Sano, Kuniaki; Masuoka, Noriyoshi; Kira, Shohei.

In: Biochimica et Biophysica Acta - Gene Structure and Expression, Vol. 1522, No. 3, 30.12.2001, p. 217-220.

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

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abstract = "Mutant catalase cDNAs from the hypocatalasemic and acatalasemic mice were cloned and expressed in bacteria. A novel missense mutation, Asp (AAT) to Ser (AGT), was identified at amino acid position 439 of the hypocatalasemic catalase. Analysis of recombinant catalase mutants revealed that the mutation is responsible for the reduced activity of hypocatalasemic catalase and the unstable tetrameric structure of acatalasemic catalase was also suggested.",

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author = "Wang, {Da Hong} and Ken Tsutsui and Kuniaki Sano and Noriyoshi Masuoka and Shohei Kira",

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T1 - cDNA cloning and expression of mutant catalase from the hypocatalasemic mouse

T2 - Comparison with the acatalasemic mutant

AU - Wang, Da Hong

AU - Tsutsui, Ken

AU - Sano, Kuniaki

AU - Masuoka, Noriyoshi

AU - Kira, Shohei

N1 - Funding Information: This work was supported by Grants-in-Aid for Scientific Research from the Ministry of Education, Science, Sports and Culture of Japan. We thank T. Nakamura and M. Ishimaru for technical assistance.

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N2 - Mutant catalase cDNAs from the hypocatalasemic and acatalasemic mice were cloned and expressed in bacteria. A novel missense mutation, Asp (AAT) to Ser (AGT), was identified at amino acid position 439 of the hypocatalasemic catalase. Analysis of recombinant catalase mutants revealed that the mutation is responsible for the reduced activity of hypocatalasemic catalase and the unstable tetrameric structure of acatalasemic catalase was also suggested.

AB - Mutant catalase cDNAs from the hypocatalasemic and acatalasemic mice were cloned and expressed in bacteria. A novel missense mutation, Asp (AAT) to Ser (AGT), was identified at amino acid position 439 of the hypocatalasemic catalase. Analysis of recombinant catalase mutants revealed that the mutation is responsible for the reduced activity of hypocatalasemic catalase and the unstable tetrameric structure of acatalasemic catalase was also suggested.

KW - Acatalasemic mouse

KW - Catalase

KW - Hypocatalasemic mouse

KW - cDNA cloning

KW - cDNA expression

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cDNA cloning and expression of mutant catalase from the hypocatalasemic mouse: Comparison with the acatalasemic mutant

Abstract

Keywords

ASJC Scopus subject areas

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