Purification and basic properties of the aspartate aminotransferases from a variety of sources

Patricia B. Porter, Donatella Barra, Francesco Bossa, Guido Cantalupo, Shawn Doonan, Filippo Martini, David Sheehan, Susan M. Wilkinson

Research output: Contribution to journalArticlepeer-review

32 Scopus citations

Abstract

1. 1. The following aspartate aminotransferases have been isolated: cytosolic and mitochondrial isozymes from horse heart, rat liver and mouse liver, the mitochondrial isozyme from turkey liver, and the single isozymes from yeast and E. coli. 2. 2. Comparisons of the electrophoretic characteristics of the various isozymes are reported. In the case of the mitochondrial isozyme from turkey liver, studies have been made of the subforms of the protein and of its behaviour on hydrophobic chromatography. 3. 3. Studies of the distribution and stabilities of aspartate aminotransferase isozymes in homogenates of trout liver are reported.

Original languageBritish English
Pages (from-to)737-746
Number of pages10
JournalComparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
Volume69
Issue number4
DOIs
StatePublished - 1981

Fingerprint

Dive into the research topics of 'Purification and basic properties of the aspartate aminotransferases from a variety of sources'. Together they form a unique fingerprint.

Cite this