Abstract
Momordin II, a ribosome-inactivating protein from Momordica charantia seeds, was purified by a procedure involving a series of chromatographies on S-Sepharose, Sephadex G-50, CM-Sepharose, and Red Sepharose columns. Highly purified momordin II inhibited cell-free protein synthesis, released adenine from rat liver ribosomes and from DNA, and had no RNase activity.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenine / metabolism
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Animals
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Cell-Free System
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Chromatography, Agarose
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DNA, Ribosomal / drug effects
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DNA, Ribosomal / metabolism
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Liver / drug effects
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Liver / metabolism
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Liver / ultrastructure
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Plant Proteins*
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Protein Biosynthesis / drug effects
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Protein Synthesis Inhibitors / pharmacology
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Rats
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Ribonucleases / isolation & purification*
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Ribosomes / drug effects
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Ribosomes / metabolism
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Saponins / isolation & purification*
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Seeds / chemistry*
Substances
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DNA, Ribosomal
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Plant Proteins
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Protein Synthesis Inhibitors
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Saponins
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momordin II (protein)
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Ribonucleases
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Adenine