Hiriyanna, K. T. ; Ramakrishnan, T. (1981) Purification and properties of a DNA polymerase from Mycobacterium tuberculosis H37Rv Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 652 (2). pp. 274-282. ISSN 0005-2787
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Official URL: http://www.sciencedirect.com/science/article/pii/0...
Related URL: http://dx.doi.org/10.1016/0005-2787(81)90117-9
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: | Article |
|---|---|
| Source: | Copyright of this article belongs to Elsevier Science. |
| Keywords: | DNA Polymerase Purification; Exonuclease Activity; (M. Tuberculosis) |
| ID Code: | 49222 |
| Deposited On: | 19 Jul 2011 11:54 |
| Last Modified: | 19 Jul 2011 11:54 |
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