Partial purification and properties of frog liver tyrosine aminotransferase.

Hepatic tyrosine aminotransferase of the frog Rana temporaria was partially purified by (NH4)2SO4 fractionation and successive chromatography on DEAE-cellulose DE-52, Ultrogel AcA-34, DEAE-cellulose DE-52 again and, finally, hydroxyapatite. During the last step, the enzyme activity separated into tw...

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Bibliographic Details
Main Authors: Ohisalo, J J, Andersson, S M, Pispa, J P
Format: Artigo
Language:Inglês
Published: 1977
Subjects:
Research Article
Online Access:https://ncbi.nlm.nih.gov/pmc/articles/PMC1164719/
https://ncbi.nlm.nih.gov/pubmed/18134
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