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• W2049206930 abstract "A new purification scheme, involving two successive ion exchange Chromatographic steps on DEAE-cellulose and Mono-S FPLC, was developed for the isolation of the ribosome-inactivating proteins, α- and β-momorcharins, from the Chinese herb Kuquazi (seeds of Momordica charantia). This simple and rapid procedure yielded 3.1 and 1.7 mg of α- and β-momorcharins, respectively, from 2.5 g of decorticated seeds in only two days. The N-terminal amino acid sequence of β-momorcharin was found to be DVNFDLSTATAKTYTKFIED. It differed from that of α-momorcharin (DVSFRLSGADPRSYGMFIKD) in 10 out of the 20 positions investigated. Like other ribosome-inactivating proteins, the purified momorcharins showed specific N-glycosidase activity at nanomolar concentrations, when rRNA from rabbit reticulocyte lysate was used as substrate. The N-glycosidase activity of both momorcharins was optimal at pH7, not inhibited by K+ and not appreciably affected by NH4+. The activity of α-momorcharin was not drastically altered by Mn2+ but (1–10mM) Mn2+ inhibited the activity of β-momorcharin by about 40%." @default.
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• W2049206930 date "1996-08-01" @default.
• W2049206930 modified "2023-09-27" @default.
• W2049206930 title "A highly efficient procedure for purifying the ribosome-inactivating proteins α- and β-momorcharins from seeds. n-terminal sequence comparison and establishment of their n-glycosidase activity" @default.
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• W2049206930 doi "https://doi.org/10.1016/0024-3205(96)00388-8" @default.
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