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ISSN: 1948-5956

Journal of Cancer Science & Therapy
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Research Article

An Atypical DNA Polymerase Beta Overexpressed in Human Aml/Hl-60 Malignant Cells

Alexander A Bukhvostov1, Oleg A Shatalov2, Alexey P Orlov3 and Dmitry A Kuznetsov3,4*

1Department of Pharmacology, School of Pharmacy, I. M. Sechenov Moscow, State Medical University, Moscow, Russia

2Department of Life Sciences, Moscow Regional Pedagogical University, Orekhovo- Zouyevo, Moscow Province, Russia

3Department of Medicinal Nanobiotechnologies, N. I. Pirogov Russian, National Research Medical University, Moscow, Russia

4N.N. Semenov Institute for Chemical Physics, Russian Academy of Sciences, Moscow, Russia

*Corresponding Author:
Dr. Dmitry A Kuznetsov
Department of Medicinal Nanobiotechnologies
NI Pirogov Russian
National Research Medical University
Moscow, Russia
E-mail: [email protected]

Received date: January 05, 2013; Accepted date: January 18, 2013; Published date: January 21, 2013

Citation: Bukhvostov AA, Shatalov OA, Orlov AP, Kuznetsov DA (2013) An Atypical DNA Polymerase Beta Overexpressed in Human Aml/Hl-60 Malignant Cells. J Cancer Sci Ther 5:094-099. doi: 10.4172/1948-5956.1000191

Copyright: © 2013 Bukhvostov AA, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

Abstract

Human acute myeloid leukemia cells overexpresses a beta–like DNA polymerase (EC 2.7.7.7) which is found
to be a chromatin associated single subunit protein (66.5 kDa) purified by original extraction/gel filtration procedure
allowing to gain the 122,000-fold purification degree as corrected to a total cell protein. The enzyme possesses
some key DNA pol β-specific catalytic properties such as the processing of short (200n-250n) single strand DNA
sequences, activation in the presence of 200 mM KCl, resistance to N-ethyl-melamide and Aphidicolin, lack of
3’,5’-exonuclease activity, and low dTTP utilization rates (KM=0.016 mM, Kcat=0.622 (μM dTTP/min)/mg protein). A
possible significance of the unique enzyme studied as a target for its pharmaceutical inhibitors is under discussion.
This work is a full–length version of a study presented as a Poster at the OMICS managed 2nd World Congress on
Science Cancer and Therapy, Sept 10–12, 2012, San Antonio, TX.

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