Purification and characterization of riproximin from Ximenia americana fruit kernels

被引:15
作者
Bayer, Helene [1 ]
Ey, Noreen [2 ]
Wattenberg, Andreas [3 ]
Voss, Cristina [2 ]
Berger, Martin R. [1 ]
机构
[1] German Canc Res Ctr, Toxicol & Chemotherapy Unit, D-69120 Heidelberg, Germany
[2] Heidelberg Pharma AG, Dept Biochem, D-68526 Ladenburg, Germany
[3] PROTAGEN AG, D-44227 Dortmund, Germany
关键词
Riproximin; Plant lectin; Type II RIP; Ximenia americana; Chromatography; Isoforms; RIBOSOME-INACTIVATING PROTEINS; RICIN A-CHAIN; VISCUM-ALBUM; LECTINS; CLONING; SAMBUCUS; COMMUNIS; SEQUENCE; IDENTIFICATION; GENES;
D O I
10.1016/j.pep.2011.11.018
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Highly pure riproximin was isolated from the fruit kernels of Xitnenia 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). (C) 2011 Elsevier Inc. All rights reserved.
引用
收藏
页码:97 / 105
页数:9
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