PURIFICATION AND CHARACTERIZATION OF ALKALINE PHOSPHATASE FROM DOLICHOS LAB-LAB AND ITS INVITRO DEPHOSPHORYLATION ACTIVITY ON NUCLEIC ACIDS
AbstractPhosphatase serves several functions in plant metabolism including growth governance, phosphorous level control, starch breakdown etc. Alkaline phosphatases, acting at an alkaline pH 8, are a significant class of enzymes that catalyze release of phosphate esters especially. This enzyme study is so far limited only to animal source and partly to microbial sources, in terms of clinical research. Although it has been identified that plant as a source of this enzyme may be exploited, there always has been a challenge on the isolation and characterization of this enzyme and how pure it can be. This paper partly addresses the above problem, where the enzyme has been isolated from the seeds Dolichos lab-lab plant characterized and its purity was checked by HPLC. The purity obtained was 98% and the enzyme has been further analyzed for its activity on nucleic acids, which gave promising and positive results.
Article Information
53
3309-3313
689KB
1219
English
IJPSR
Praveen Kumar Vemuri*, Rama Krishna Yadam, Naga Sravani Jandhyala, Sreelekha Revur, Ramya Hari Priya Velampati and Anusha Kalapala
Center for Genomics & Proteomics, Department of Biotechnology, K. L. University, Green Fields, Vaddeswaram, Guntur District, Andhra Pradesh, India
vemuripraveen_bt@kluniversity.in
16 May, 2012
11 June, 2012
25 August, 2012
http://dx.doi.org/10.13040/IJPSR.0975-8232.3(9).3309-13
01 September, 2012
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