The complete amino acid sequence of cytoplasmic aspartate aminotransferase from pig heart

Ovchinnikov, Yu.A.; Egorov, C.A.; Aldanova, N.A.; Feigina, M.Yu.; Липкин, В. М.; Abdulaev, N.G.; Grishin, Eugene V.; Kiselev, A. P.; Modyanov, N.N.; Braunstein, A. E.; Polyanovsky, O.L.; Носиков, В. В.

doi:10.1016/0014-5793(73)80008-0

Cited by 207 publications

(99 citation statements)

References 12 publications

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“…We have recently reported the complete primary structure of cytoplasmic AAT from pig heart [3 ] ; similar results were obtained by Ovchinnikov et al [4]. To establish the structural and evolutionary relationships between the cytoplasmic and mitochondrial isozymes, we are now carrying out studies of the amino acid sequence of the mitochondrial form.…”

Section: Introductionsupporting

confidence: 70%

Homology of the primary structures of cytoplasmic and mitochondrial aspartate aminotransferases from pig heart

Doonan¹,

Hughes²

1974

FEBS Letters

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Section: Introductionsupporting

confidence: 70%

Homology of the primary structures of cytoplasmic and mitochondrial aspartate aminotransferases from pig heart

Doonan¹,

Hughes²

1974

FEBS Letters

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“…The isozymes of aspartate aminotransferase differ from one another in chemical, physical, catalytic and immunochemical properties (for a review, see [4]). The primary structure of the cytoplasmic enzyme from pig heart has now been established [5,6] and it therefore seemed of interest to carry out similar studies on the mitochondrial form to establish whether the structures are related and if so, the degree of homology between them; this information is not available for any other pair of cytoplasmic and mitochondrial isozymes. Our preliminary results showed that the structures are indeed related [7] and this conclusion has been independently confirmed [8,9].…”

mentioning

confidence: 99%

Large-Scale Purification and Some Properties of the Mitochondrial Aspartate Aminotransferase from Pig Heart

Barra

Bossa

Doonan³

et al. 1976

Eur J Biochem

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A method has been developed which allows isolation of 0.3 -0.5 g of mitochondrial aspartate aminotransferase in five days starting from 10 pig hearts; the method does not involve initial preparation of mitochondria. Mitochondrial malate dehydrogenase and the cytoplasmic aspartate aminotransferase may conveniently be recovered from side fractions. The product mitochondrial aspartate aminotransferase is homogeneous as judged by various electrophoretic techniques and by N-terminal analysis. Crystals of the enzyme have been obtained both from concentrated, essentially salt-free, solutions and from solutions of ammonium sulphate. The amino acid composition, N and C-terminal amino acid sequences and subunit molecular weight have been determined; these characteristic properties are compared with those of the cytoplasmic isozyme from the same source.Aspartate aminotransferase is one of a small group of enzymes the members of which exist in tissues of higher organisms in two distinct forms, one associated with the soluble fraction and the other with mitochondria [ l -31. The isozymes of aspartate aminotransferase differ from one another in chemical, physical, catalytic and immunochemical properties (for a review, see [4]). The primary structure of the cytoplasmic enzyme from pig heart has now been established [5,6] and it therefore seemed of interest to carry out similar studies on the mitochondrial form to establish whether the structures are related and if so, the degree of homology between them; this information is not available for any other pair of cytoplasmic and mitochondrial isozymes. Our preliminary results showed that the structures are indeed related [7] and this conclusion has been independently confirmed [8,9].Existing methods for isolation of the mitochondrial isozyme [4,10] started from preparations of intact mitochondria and were not suitable for large scale work. We have developed a new method, starting from whole-cell homogenates, which exploits the cationic properties of the mitochondrial isozyme and allows rapid isolation of the protein in quantities sufficient Ahbreviufion. Dansyl, 5-dimethylaminonaphthalene-l-sulphonyl.Enzymes. Aspartate aminotransferase (EC 2.6

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“…40) In addition, the seven other invariant residues in family I aminotransferase (Y70, P195, N194, P195, Y225, R266, and G268, the numbers of which are according to cytosolic pig AspAT) were also conserved in YfbQ and YfdZ. 41,42) The functional roles of these conserved residues are known to be binding with substrates and cofactor PLP.…”

Section: Discussionmentioning

confidence: 99%

Isolation of a Mutant Auxotrophic forL-Alanine and Identification of Three Major Aminotransferases That SynthesizeL-Alanine inEscherichia coli

Yoneyama

Hori

Lim

et al. 2011

Bioscience, Biotechnology, and Biochemistry

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The complete amino acid sequence of cytoplasmic aspartate aminotransferase from pig heart

Cited by 207 publications

References 12 publications

Homology of the primary structures of cytoplasmic and mitochondrial aspartate aminotransferases from pig heart

Homology of the primary structures of cytoplasmic and mitochondrial aspartate aminotransferases from pig heart

Large-Scale Purification and Some Properties of the Mitochondrial Aspartate Aminotransferase from Pig Heart

Isolation of a Mutant Auxotrophic forL-Alanine and Identification of Three Major Aminotransferases That SynthesizeL-Alanine inEscherichia coli

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