Curcin C, a novel type I ribosome-inactivating protein from the post-germinating cotyledons of Jatropha curcas
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, resp...
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Published in: | Amino acids Vol. 49; no. 9; pp. 1619 - 1631 |
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Main Authors: | , , , , , , , , |
Format: | Journal Article |
Language: | English |
Published: |
Vienna
Springer Vienna
01-09-2017
Springer Nature B.V |
Subjects: | |
Online Access: | Get full text |
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Summary: | 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 IC
50
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. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0939-4451 1438-2199 |
DOI: | 10.1007/s00726-017-2456-8 |