Curcin C, a novel type I ribosome-inactivating protein from the post-germinating cotyledons of Jatropha curcas

Curcin C, a novel type I ribosome-inactivating protein from the post-germinating cotyledons of... A novel type I ribosome-inactivating protein (RIP), designated as curcin C, was purified from Jatropha curcas, an important feedback source of bio-fuel. Molecular mass and isoelectric point of curcin C were 31.398 kDa and 7.12 as detected by MALTI-TOF assay and capillary electrophoresis assay, respectively. N-terminal sequence and LC–MS/MS analyses confirmed that curcin C is a type I RIP having high homology, but not the exactly the same with curcin, another type 1 RIP isolated from the endosperm of J. curcas. It exhibited N-glycosidase activity and in vitro translation inhibition activity. Moreover, curcin C displayed a strong selectively anti-tumor activity on human cancer cells. Its cytotoxicity against osteosarcoma cell line U20S is even higher than that of Paclitaxel with IC50 of 0.019 μM. Purification and identification of curcin C not only suggested its potential in natural anticancer drug development, but also provide chance to understanding different cytotoxic action among different RIPs. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Amino Acids Springer Journals

Curcin C, a novel type I ribosome-inactivating protein from the post-germinating cotyledons of Jatropha curcas

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Publisher
Springer Vienna
Copyright
Copyright © 2017 by Springer-Verlag GmbH Austria
Subject
Life Sciences; Biochemistry, general; Analytical Chemistry; Biochemical Engineering; Life Sciences, general; Proteomics; Neurobiology
ISSN
0939-4451
eISSN
1438-2199
D.O.I.
10.1007/s00726-017-2456-8
Publisher site
See Article on Publisher Site

Abstract

A novel type I ribosome-inactivating protein (RIP), designated as curcin C, was purified from Jatropha curcas, an important feedback source of bio-fuel. Molecular mass and isoelectric point of curcin C were 31.398 kDa and 7.12 as detected by MALTI-TOF assay and capillary electrophoresis assay, respectively. N-terminal sequence and LC–MS/MS analyses confirmed that curcin C is a type I RIP having high homology, but not the exactly the same with curcin, another type 1 RIP isolated from the endosperm of J. curcas. It exhibited N-glycosidase activity and in vitro translation inhibition activity. Moreover, curcin C displayed a strong selectively anti-tumor activity on human cancer cells. Its cytotoxicity against osteosarcoma cell line U20S is even higher than that of Paclitaxel with IC50 of 0.019 μM. Purification and identification of curcin C not only suggested its potential in natural anticancer drug development, but also provide chance to understanding different cytotoxic action among different RIPs.

Journal

Amino AcidsSpringer Journals

Published: Jun 29, 2017

References

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