| Literature DB >> 22178181 |
Helene Bayer1, Noreen Ey, Andreas Wattenberg, Cristina Voss, Martin R Berger.
Abstract
Highly pure riproximin was isolated from the fruit kernels of Ximenia americana, a defined, seasonally available and potentially unlimited herbal source. The newly established purification procedure included an initial aqueous extraction, removal of lipids with chloroform and subsequent chromatographic purification steps on a strong anion exchange resin and lactosyl-Sepharose. Consistent purity and stable biological properties were shown over several purification batches. The purified, kernel-derived riproximin was characterized in comparison to the African plant material riproximin and revealed highly similar biochemical and biological properties but differences in the electrophoresis pattern and mass spectrometry peptide profile. Our results suggest that although the purified fruit kernel riproximin consists of a mixture of closely related isoforms, it provides a reliable basis for further research and development of this type II ribosome inactivating protein (RIP). Copyright ÂEntities:
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Year: 2011 PMID: 22178181 DOI: 10.1016/j.pep.2011.11.018
Source DB: PubMed Journal: Protein Expr Purif ISSN: 1046-5928 Impact factor: 1.650