Open Access5′‐Hydroxyl RNA kinase from mouse L cells
Author(s) -
SERTICPRITSOS Karen,
VINOCOUR Michelle,
WINICOV Ilga
Publication year - 1984
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1984.tb08429.x
Subject(s) - chemistry , microbiology and biotechnology , rna , biology , biochemistry , gene
A 5′‐hydroxyl RNA kinase from mouse L cells has been partially purified and characterized. The enzyme transfers the γ‐phosphorus from ATP to 5′‐hydroxyl termini of RNA much more efficiently than DNA substrates, and is virtually inactive on 3′‐CMP. The molecular mass of the predominant kinase activity is estimated to be 93–96 kDa from denaturing and non‐denaturing polyacrylamide gel analyses. A minor band of lower molecular mass has been also observed. The enzyme activity requires Mg 2+ and is inhibited by both Mn 2+ and Zn 2+ . Antibodies to small nuclear ribonucleoproteins have no effect on this activity.