Affordable Access

Publisher Website

Tyrosine aminotransferase from rat liver, a purification in three steps

Authors
Journal
Biochemical and Biophysical Research Communications
0006-291X
Publisher
Elsevier
Publication Date
Volume
80
Issue
4
Identifiers
DOI: 10.1016/0006-291x(78)91311-6
Disciplines
  • Biology

Abstract

Abstract Tyrosine aminotransferase from rat liver was isolated by a three step purification method involving affinity chromatography, CM-50 chromatography and G-200 gel filtration. In order to synthesize the affinity gel, the coenzyme pyridoxamine-5′-phosphate was coupled via a spacer group to a sepharose matrix. The enzyme preparation showed a single band in SDS-acrylamide gel electrophoresis and contains three multiple enzyme forms. A molecular weight of 50,000 of the tyrosine aminotransferase subunit was estimated.

There are no comments yet on this publication. Be the first to share your thoughts.