Indranil Chanda1 
,
Sanat Kumar Basu2,
Sadhan Kumar Dutta3,
Smriti Rekha Chanda Das1
For correspondence:- Indranil Chanda Email: ichanda@sify.com Tel:+919957179226
Received: 12 May 2011 Accepted: 15 October, 2011 Published: 25 December 2011
Citation: Chanda I, Basu SK, Dutta SK, Chanda Das SR. A Protease Isolated from the Latex of Plumeria rubra Linn (Apocynaceae) 1: Purification and Characterization. Trop J Pharm Res 2011; 10(6):705-711 doi: 10.4314/tjpr.v10i6.2
© 2011 The authors.
This is an Open Access article that uses a funding model which does not charge readers or their institutions for access and distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0) and the Budapest Open Access Initiative (http://www.budapestopenaccessinitiative.org/read), which permit unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited..
Purpose: To isolate, purify and characterize protease from the latex of the plant.
Methods: Protease was isolated from the latex of Plumeria rubra Linn using acetone precipitation method and purified by a sequence of DEAE cellulose column chromatography, followed by two successive column purification in Sephadex G-50 and Sephadex G-200. The molecular weight of the purified protease was determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The protease was given a trivial name, Plumerin-R.
Results: Plumerin-R showed a single protein band on SDS-PAGE and molecular weight was approximately 81.85 kDa. It remained active over a broad range of temperature but had optimum activity at 55 °C and pH 7.0 when casein was used as substrate. Activation of the protease by a thiol-activating agent indicated the presence of sulfhydryl as an essential group for its activity.
Conclusion: A protease from the latex of Plumeria rubra Linn was purified to homogeneity by a simple purification procedure and then characterized.
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