| Literature DB >> 1672893 |
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.Entities:
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Year: 1991 PMID: 1672893 DOI: 10.1111/j.2042-7158.1991.tb06642.x
Source DB: PubMed Journal: J Pharm Pharmacol ISSN: 0022-3573 Impact factor: 3.765