Purification and characterization of cold-active L-glutamate dehydrogenase independent of NAD(P) and oxygen.

Purification and characterization of cold-active L-glutamate dehydrogenase independent of NAD(P) and oxygen. Research Abstract Details 

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Purification and characterization of cold-active L-glutamate dehydrogenase independent of NAD(P) and oxygen. Abstract Text:

A Yamamura,T Sakaguchi,Y Murakami,K Yokoyama,E Tamiya,

L-Glutamate dehydrogenase (GLDH) independent of NAD(P) and oxygen was first obtained from the psychrotrophic bacterium Aeromonas sp. L101, originally isolated from the organs of salmon (Oncorhynchus keta). GLDH was purified by a series of chromatography steps on DEAE-Sepharose, Superdex 200pg, Q-Sepharose, CM-Sepharose, and Phenyl-Sepharose. The purified protein was determined to have a molecular mass of 110 kDa and a pI of 5.7. Maximum activity was obtained at 55 degrees C and pH 8.5. The activity of GLDH at 4 and 20 degrees C was 38 and 50%, respectively, of that at 50 degrees C. GLDH was coupled to cytochrome c and several redox dyes including 1-methoxy-5-methylphenazinium methylsulfate (1-Methoxy PMS), 2, 6-dichlorophenylindophenol (DCIP), 9-dimethylaminobenzo[alpha]phenoxazin-7-ium chloride (meldola's blue), 3,3'-[3,3'-dimethoxy-(1,1'-biphenyl)-4, 4'-diyl]-bis[2-(4-nitrophenyl)-5-phenyl-2H tetrazolium chloride] (nitroblue tetrazolium; NBT), and 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyl-2H tetrazolium (INT). The presence of NAD(P) and oxygen gave no oxidation activity to GLDH. Spectroscopic profile and ICP data indicated a b-type cytochrome containing iron.

Purification and characterization of cold-active L-glutamate dehydrogenase independent of NAD(P) and oxygen. Publishing Authors By Initials

A Yamamura,T Sakaguchi,Y Murakami,K Yokoyama,E Tamiya,

For similar environment and public health: environment: environment, controlled: temperature research abstracts see: environment and public health: environment: environment, controlled: temperature research

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Purification and characterization of cold-active L-glutamate dehydrogenase independent of NAD(P) and oxygen. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 125

Page Numbers: 760-9

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Apr

YEAR: 1999

Purification and characterization of cold-active L-glutamate dehydrogenase independent of NAD(P) and oxygen. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Purification and characterization of cold-active L-glutamate dehydrogenase independent of NAD(P) and oxygen. Keywords Mesh Terms:

KEYWORDS: Temperature

MESH TERMS: microbiology

Chemical & Substance for Abstract: Purification and characterization of cold-active L-glutamate dehydrogenase independent of NAD(P) and oxygen. Information

Substance Name: Glutamate Dehydrogenase

Registry Number: EC 1.4.1.2

Grant and Affiliation Information for Purification and characterization of cold-active L-glutamate dehydrogenase independent of NAD(P) and oxygen.

AFFILIATION: School of Materials Science, Japan Advanced Institute of Science & Technology, Tatsunokuchi, Ishikawa, 923-1292, Japan. yamamura@jaist.ac.jp.

Country: JAPAN

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MEDLINETA: J Biochem

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