Volume 13, No 5, Oct 2003

ISSN: 1001-0602 
EISSN: 1748-7838 2018 
impact factor 17.848* 
(Clarivate Analytics, 2019)

Volume 13 Issue 5, October 2003: 369-374

ORIGINAL ARTICLES

Purification and characterization of Moschatin, a novel type I ribosome-inactivating protein from the mature seeds of pumpkin (Cucurbita moschata), and preparation of its immunotoxin against human melanoma cells

HENG CHUAN XIA, FENG LI, ZHEN LI, ZU CHUAN ZHANG*

Key Laboratory of Proteomics, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China. E-mail: zhangzc@sunm.shcnc.ac.cn Correspondence: Zu Chuan ZHANG(zhangzc@sunm.shcnc.ac.cn )

A novel ribosome-inactivating protein designated Moschatin from the mature seeds
of pumpkin (Cucurbita moschata) has been successively purified to homogeneity,
using ammonium sulfate precipitation, CM-cellulose 52 column chromatography,
Blue Sepharose CL-6B Affinity column chromatography and FPLC size-exclusion
column chromatography. Moschatin is a type 1 RIP with a pI of 9.4 and molecular
weight of ~29 kD. It is a rRNA N-glycosidase and potently blocked the protein
synthesis in the rabbit reticulocyte lysate with a IC₅₀ of 0.26 nM.
Using the anti-human melanoma McAb Ng76, a novel immunotoxin Moschatin-Ng76
was prepared successfully and it efficiently inhibited the growth of targeted
melanoma cells M₂₁ with a IC₅₀ of 0.04 nM, 1500
times lower than that of free Moschatin. The results implied that Moschatin
could be used as a new potential anticancer agent.

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