Purification and characterization of glucose 6-phosphate dehydrogenase from the liver of pearl spot (etroplus suratensis)

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dc.contributor.authorMathew, P.T.
dc.contributor.authorGopakumar, K.
dc.date.accessioned2014-01-04T09:01:27Z
dc.date.available2014-01-04T09:01:27Z
dc.date.issued1993
dc.description.abstractGlucose-6-phosphate dehydrogenase was purified from the liver of the fish pearl spot (Etroplus suratensis) by buffer extraction, ammonium sulphate fractionation and chromatography on DEAE cellulose and Sephadex G100. The preparation was homogeneĀ­ous on polyacrylamide disc gel electrophoresis and on gel filtration through Sephacryl S-200. The enzyme is a dimer and showed a molecular weight of 118 000- 120 000. The temperature and pH optima of the purified enzyme were 37 degree C and 8 degree C respectively. It remained stable at temperatures of 20-50 degree C and at pH 6.5-8.4. Km values obtained were 105 micro M with respect to the substrate glucose-6-phosphate and 50 micro M with respect to NA DP. The effect of halogens, various metal ions and palmitoyl coenzyme A on enzyme activity, substrate specificity and amino acid composition are also reported.en_US
dc.identifier.citationJournal of Tropical Science 1993: 33, 166-181en_US
dc.identifier.urihttp://hdl.handle.net/123456789/1267
dc.language.isoenen_US
dc.publisherTropical Products Institute (Great Britain), John Wiley & Sonsen_US
dc.subjectGlucose-6-phosphateen_US
dc.subjectdehydrogenaseen_US
dc.subjectpearl spoten_US
dc.titlePurification and characterization of glucose 6-phosphate dehydrogenase from the liver of pearl spot (etroplus suratensis)en_US
dc.typeArticleen_US
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