title: Extraction and purification of curcain, a protease from the latex of Jatropha curcas Linn.
abstract: A proteolytic enzyme, curcain, has been extracted from the latex of Jatropha curcas Linn. The enzyme was purified by chromatography on carboxymethyl cellulose and gel filtration on Sephadex G-200. The homogeneity of protein associated with curcain was established by non-denatured polyacrylamide gel electrophoresis using a discontinuous buffer system. The molecular weight of curcain was estimated by Sephadex G-100 gel filtration using a calibration curve of standard proteins to be around 22,000 daltons.
authors.affiliation: Department of Pharmaceutical Sciences, Dibrugarh University, India.
authors.forename: L K
authors.initials: LK
authors.lastname: Nath
authors.forename: S K
authors.initials: SK
authors.lastname: Dutta
mesh_terms: D002850:Chromatography, Gel; D004589:Electrophoresis, Disc; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000032:analysis; D007840:Latex / Q000032:analysis*; D010447:Peptide Hydrolases / Q000302:isolation & purification*; D010936:Plant Extracts / Q000302:isolation & purification*
chemical_list: D007840:Latex; D010936:Plant Extracts; D010450:Endopeptidases; D010447:Peptide Hydrolases