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Purification and properties of a DNA polymerase from Mycobacterium tuberculosis H37Rv

Hiriyanna, KT and Ramakrishnan, T (1981) Purification and properties of a DNA polymerase from Mycobacterium tuberculosis H37Rv. In: Biochimica et Biophysica Acta (BBA), 652 (2). pp. 274-282.

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Abstract

DNA polymerase has been purified approximately 2000-fold from Mycobacterium tuberculosis H37Rv. The purified preparation was homogeneous by electrophoretic criteria and has a molecular weight of 135 000. The purified enzyme resembles Escherichia coli polymerase I in its properties, being insensitive to sulfhydryl drugs and possessing 5′,3′-exonuclease activity in addition to polymerase and 3′,5′-exonuclease activities. However, it differs from the latter in its sensitivity to higher salt concentration and DNA intercalating agents such as 8-aminoquinoline. The polymerase exhibited maximal activity between 37–42°C and pH 8.8–9.5. The polymerase was stable for several months below 0°C. However, the 5′,3′-exonuclease activity was more labile. The effects of different metal ions, polyamines and drugs on the polymerase activity are presented.

Item Type: Journal Article
Additional Information: Copyright of this article belongs to Elsevier Science.
Department/Centre: Division of Biological Sciences > Microbiology & Cell Biology
Date Deposited: 23 Dec 2009 07:41
Last Modified: 19 Sep 2010 05:47
URI: http://eprints.iisc.ernet.in/id/eprint/23859

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