Crystallization and properties of human liver ornithine aminotransferase.

Crystallization and properties of human liver ornithine aminotransferase. Research Abstract Details 

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Crystallization and properties of human liver ornithine aminotransferase. Abstract Text:

T Ohura,E Kominami,K Tada,N Katunuma,

Ornithine aminotransferase [EC 2.6.1.13] was purified and crystallized from human liver by a procedure involving heat treatment, chromatographies on DEAE-cellulose, Octyl-Sepharose CL-4B and Sephadex G-200, and crystallization. The purified enzyme appeared to be homogeneous on polyacrylamide gel electrophoresis with and without sodium dodecyl sulfate. The molecular weight of the enzyme was estimated as 44,000 by sodium dodecyl sulfate electrophoresis and as 177,000 by sucrose density gradient centrifugation, indicating that the enzyme is tetrameric. Various properties of the enzyme from human liver are similar to those of the enzyme from rat liver, including its molecular weight, pH optimum, Km values for ornithine, alpha-ketoglutarate and pyridoxal phosphate and specificity for amino acceptor from ornithine. The amino acid compositions of the two enzymes also have certain similarities, but the enzymes differ in electrophoretic mobility and antigenicity: the human enzyme moved more slowly to the anode, and on immunodiffusion analysis, the single precipitin lines formed between anti-human enzyme serum or anti-rat liver enzyme and the enzyme from human liver or lymphoblastoid cells and the rat liver enzyme fused with spur formation.

Crystallization and properties of human liver ornithine aminotransferase. Publishing Authors By Initials

T Ohura,E Kominami,K Tada,N Katunuma,

For similar enzymes and coenzymes: enzymes: transferases: nitrogenous group transferases: transaminases research abstracts see: enzymes and coenzymes: enzymes: transferases: nitrogenous group transferases: transaminases research

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Crystallization and properties of human liver ornithine aminotransferase. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 92

Page Numbers: 1785-92

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Dec

YEAR: 1982

Crystallization and properties of human liver ornithine aminotransferase. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Crystallization and properties of human liver ornithine aminotransferase. Keywords Mesh Terms:

KEYWORDS: Transaminases

MESH TERMS: metabolism

Chemical & Substance for Abstract: Crystallization and properties of human liver ornithine aminotransferase. Information

Substance Name: Ornithine-Oxo-Acid Transaminase

Registry Number: EC 2.6.1.13

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Country: JAPAN

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MEDLINETA: J Biochem

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