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Biochem Cell Biol. 1996;74(1):67-73.

Purification and characterization of the double-stranded DNA-activated protein kinase, DNA-PK, from human placenta.

Author information

1
Department of Biological Sciences, University of Calgary, Canada.

Abstract

The double-stranded DNA-activated protein kinase (DNA-PK) is a serine-threonine protein kinase that is composed of a large catalytic subunit (p350) and a DNA-binding protein of 70 and 80 kDa subunits known as the Ku autoantigen. When targeted to DNA by free DNA ends, DNA-PK phosphorylates many DNA-binding proteins and transcription factors. Previously, DNA-PK had only been purified and characterized from transformed human tissue culture cells. Here we report that DNA-PK is an abundant protein in human placenta and lymphocytes. We have purified the placental DNA-PK to homogeneity and show that its biochemical properties are similar to those of the HeLa cell enzyme.

PMID:
9035691
DOI:
10.1139/o96-007
[Indexed for MEDLINE]

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