Purification and characterization of the protein kinase eEF-2 isolated from rat liver cells.

A Gajko; W Gałasiński; A Gindzieński

doi:10.18388/abp.1994_4687

Purification and characterization of the protein kinase eEF-2 isolated from rat liver cells.

A Gajko Department of General and Organic Chemistry, Medical Academy, Białystok, Poland.;
W Gałasiński
A Gindzieński

DOI: https://doi.org/10.18388/abp.1994_4687

Abstract

The elongation factor 2 (eEF-2) protein kinase was isolated from rat liver cells, purified and partly characterized. It was found that the enzyme exists in an inactive form in the homogenate of rat liver. The active fraction of kinase eEF-2 was obtained after removal of the inhibitory substance by hydroxyapatite column chromatography. The purified enzyme is an electrophoretically homogeneous protein with relative molecular mass of approximately 90,000 and isoelectric point, pI = 5.9. The enzyme specifically phosphorylates the elongation factor eEF-2 in the presence of calmodulin and Ca2+.

Published

1994-12-31

Issue

Vol. 41 No. 4 (1994)

Section

Articles

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