Affordable Access

Publisher Website

Purification and subunit structure of phenylalanyl-tRNA synthetase from hen liver mitochondria

Authors
Journal
Biochemical and Biophysical Research Communications
0006-291X
Publisher
Elsevier
Publication Date
Volume
106
Issue
2
Identifiers
DOI: 10.1016/0006-291x(82)91113-5
Disciplines
  • Biology

Abstract

Abstract Hen liver mitochondrial phenylalanyl-tRNA synthetase is purified to homogeneity by a series of steps including salting-out chromatography, salting-out affinity chromatography in the presence of tRNA Phe, dissociation of the enzyme-tRNA complex on DEAE-cellulose, chromatography on DEAE-Sepharose CL-6B and Sepharose 6B. The enzyme appears to be a tetrameric enzyme with a molecular weight of 255 000, as determined by gel filtration, with a subunit structure of α 2β 2 (α = 57 000, β = 66 000), as determined by sodium dodecyl sulfate gel electrophoresis.

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