Extraction and Purification of Curcain, a Protease from the Latex of Jatropha curcas Linn
- 1 February 1991
- journal article
- Published by Oxford University Press (OUP) in Journal of Pharmacy and Pharmacology
- Vol. 43 (2) , 111-114
- https://doi.org/10.1111/j.2042-7158.1991.tb06642.x
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 22000 daltons.Keywords
This publication has 11 references indexed in Scilit:
- [16] Preparation of buffers for use in enzyme studiesPublished by Elsevier ,2004
- Irritant phorbol derivatives from four Jatropha speciesPhytochemistry, 1984
- PHYTOCHEMICAL STUDY OFJATROPHA CURCASPlanta Medica, 1977
- Flavonoids of some euphorbiaceous plantsPhytochemistry, 1971
- DISC ELECTROPHORESIS – II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS*Annals of the New York Academy of Sciences, 1964
- DISC ELECTROPHORESIS‐I BACKGROUND AND THEORY*Annals of the New York Academy of Sciences, 1964
- Estimation of the molecular weights of proteins by Sephadex gel-filtrationBiochemical Journal, 1964
- Determination of Molecular Weights of Proteins by Gel Filtration of Sephadex.Analytical Chemistry, 1963
- [1] Column chromatography of proteins: Substituted cellulosesPublished by Elsevier ,1962
- CRYSTALLINE SOYBEAN TRYPSIN INHIBITORThe Journal of general physiology, 1947