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Partial Purification and Characterization of Conus textile Venom Phosphodiesterase I​

The Bulletin of Philippine Biochemical Society
​Volume 7, Issue 2, 1987, Pages 44-50
                                                          
Authors
Ramon R. Miranda, Milagros B. Leano and Angelita G. Reyes* 

MB Leano & AG Reyes, Dept. of Biochemistry and Molecular Biology, College of Medicine, University of the Philippines - Manila; RR Miranda, Massachusetts Institute of Technology, USA
*To whom correspondence should be addressed

Abstract                                              
         Phosphodiesterae I (5’ exonuclease, E.C. 3.1.4.1) was isolated and purified to apparent homogeneity from the venom of Conus textile by a series of differential extractions and chromatographies using Sepharose 4B, DEAE-cellulose 4B and DEAE-Sephadex column. The Mr of the enzyme obtained through Sepharose 4B chromatography was estimated at 1,200,000. SDS polyacrylamide gel electrophoresis set the main subunit Mr at 60,000. The optimum conditions for the assay with para-nitrophenyl thymidine-5’-phosphate as substrate were pH 8.8, temperature at 40°C and a 40 mM magnesium ion concentration in a buffer of high ionic strength. The pI determined by isoelectric focusing was about 7.8-7.9. The Eadie-Hofstee diagnostic plot gave values of Km = 3.7 x 10-3 M and Vmax = 608 µmoles p-nitrophenol liberated/mg protein/min. EDTA in a 0.01 M concentration was found to moderately inhibit the enzyme reaction.​

To cite this article
R.R. Miranda, M.B. Leano and A.G. Reyes​, Partial Purification and Characterization of Conus textile Venom Phosphodiesterase I, The Bulletin of Philippine Biochemical Society, Vol. 7, No. 2, 1987, pp. 44-50. 
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