Sae , S.W. and Kadoum, A.M. and Cunningham, B.A. (1971) Purification and some properties of sorghum grain esterase and peroxidase. Phytochemistry, 10 (1). pp. 1-8.
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Abstract
A carboxylesterase from sorghumgrain was partially purified by (NH4)2SO4 fractionation and Sephadex G-100 gel filtration. A 72 fold purification was obtained with 28% yield. The enzyme was identified as carboxylic ester hydrolase, (E.C. 3.1.1.1) by studying the inhibition response to DFP, eserine, and PCMB. A mol. wt. of 60,000 was determined by gel filtration. The isoelectric point at pH 6·6 was revealed from a single peak in a focusing electrophoresis gradient; however, two isoenzymes were observed on agarose gel electrophoresis at pH 5·5. These isoenzymes reacted differently with DFP and paraoxon. A peroxidase was also detected in the sorghumgrain extract. Isoelectric focusing showed two basic peroxidase isoenzymes immobile at pH 9·0 and 10·0. A single peroxidase peak on gel filtration gave mol. wt. 43,000
| Item Type: | Article |
|---|---|
| Author Affiliation: | Department of Entomology and Department of Biochemistry, Kansas State University, Manhattan, Kansas 66502, U.S.A. |
| Subjects: | Plant Protection |
| Divisions: | Sorghum |
| Depositing User: | Ms K Syamalamba |
| Date Deposited: | 21 Aug 2012 10:56 |
| Last Modified: | 21 Aug 2012 10:57 |
| Official URL: | http://dx.doi.org/10.1016/S0031-9422(00)90243-7 |
| URI: | http://eprints.icrisat.ac.in/id/eprint/7445 |
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