Purification and characterisation of a carboxylesterase from the latex of Synadenium grantii Hook,'f'
作者： T. Govindappa , L. Govardhan , P. S. Jyothy , P. S. Veerabhadrappa
DOI: 10.1007/BF02716956
关键词:
摘要: The latex ofSynadenium grantii was found to contain esterolytic activity. Polyacrylamide gel electrophoretic study coupled with substrate and inhibitor specificity studies revealed the presence of multiple forms carboxylesterases cholinesterases in latex. One purified by acetone fractionation, carboxymethyl-Sephadex chromatography Sepharose-6B filtration. homogeneity enzyme established polyacrylamide electrophoresis, isoelectric focussing sodium dodecyl sulphate-polyacrylamide electrophoresis. consists a single polypeptide chain molecular weight 14,000. amino acid analysis that it contained greater number neutral acidic, compared basic residues. pH be 4.0. glycoprotein as periodic Schiff-staining technique. Studies different organophosphate carbamate inhibitors showed this sensitive organophosphates. product inhibition linear competitive acetate non-competitive 1-naphthol.
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