Journal article

Authors list: RUSCAK, M; ORLICKY, J; ZUBOR, V; HAGER, H

Publication year: 1982

Pages: 210-216

Journal: Journal of Neurochemistry

Volume number: 39

Issue number: 1

ISSN: 0022-3042

eISSN: 1471-4159

DOI Link: https://doi.org/10.1111/j.1471-4159.1982.tb04720.x

Publisher: Wiley

Abstract: 
Mitochondrial and cytosolic alanine aminotransferases (EC 2.6.1.2) were partially purified (140- and 180-fold, respectively) from bovine brain cortex by means of (NH4)2SO4 precipitation, gel filtration on Sephadex G-150 and ion-exchange chromatography on DEAE A-50 and were characterized. The enzymes exhibited identicl MW (110,000 .+-. 10,000) and pH optima (7.8), but were eluted from CM Sephadex C-50 at different ionic strengths. Isoelectric focusing of the enzymes indicated a pI value of 5.2 for the cytosolic enzyme and 7.2 for the mitochondrial enzyme. The Km values of the mitochondrial enzyme were 5.1, 6.6, 0.7 and 0.4 mM and of the cytosolic isozyme were 30.3, 4.3, 0.7 and 0.5 mM for alanine, glutamate, 2-oxoglutarate and pyruvate, respectively. Evidently, forms of alanine aminotransferase exist in nerve tissue, which suggests that they may play different roles in the cellular metabolism of nerve tissue.

Harvard Citation style: RUSCAK, M., ORLICKY, J., ZUBOR, V. and HAGER, H. (1982) ALANINE AMINOTRANSFERASE IN BOVINE BRAIN - PURIFICATION AND PROPERTIES, Journal of Neurochemistry, 39(1), pp. 210-216. https://doi.org/10.1111/j.1471-4159.1982.tb04720.x

APA Citation style: RUSCAK, M., ORLICKY, J., ZUBOR, V., & HAGER, H. (1982). ALANINE AMINOTRANSFERASE IN BOVINE BRAIN - PURIFICATION AND PROPERTIES. Journal of Neurochemistry. 39(1), 210-216. https://doi.org/10.1111/j.1471-4159.1982.tb04720.x