Literature DB >> 4030726

Aspartate aminotransferase isozymes from rabbit liver. Purification and properties.

S Kuramitsu, K Inoue, K Kondo, K Aki, H Kagamiyama.   

Abstract

Cytosolic and mitochondrial isozymes of aspartate aminotransferase (L-aspartate:2-oxoglutarate aminotransferase [EC 2.6.1.1] ) were purified to homogeneity from rabbit liver. The rabbit liver isozymes were closely similar to the corresponding isozymes from other sources, including human heart, pig heart, chicken heart, and rat liver, in their molecular weights, absorption spectra, amino acid compositions, isoelectric points, and Michaelis constants for the substrates. The NH2-terminal amino acid sequences of rabbit liver isozymes were identified up to 30 residues, and showed some differences from those of the corresponding isozymes obtained from other animals so far studied.

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Year:  1985        PMID: 4030726     DOI: 10.1093/oxfordjournals.jbchem.a135186

Source DB:  PubMed          Journal:  J Biochem        ISSN: 0021-924X            Impact factor:   3.387


  5 in total

1.  Purification and characterization of aspartate aminotransferase from the halophile archaebacterium Haloferax mediterranei.

Authors:  F J Muriana; M C Alvarez-Ossorio; A M Relimpio
Journal:  Biochem J       Date:  1991-08-15       Impact factor: 3.857

2.  [Isoenzymes].

Authors:  G Pfleiderer
Journal:  Naturwissenschaften       Date:  1986-11

3.  Kinetic model of mitochondrial Krebs cycle: unraveling the mechanism of salicylate hepatotoxic effects.

Authors:  Ekaterina Mogilevskaya; Oleg Demin; Igor Goryanin
Journal:  J Biol Phys       Date:  2006-10-26       Impact factor: 1.365

4.  Generation process of cytosolic aspartate aminotransferase molecular forms by several treatments.

Authors:  S Imperial; C Quiroga; M Busquets; A Cortés; J Bozal
Journal:  J Protein Chem       Date:  1988-04

5.  The Kinetics of Enzyme Mixtures.

Authors:  Simon Brown; Noorzaid Muhamad; Kevin C Pedley; David C Simcock
Journal:  Mol Biol Res Commun       Date:  2014-03
  5 in total

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