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Protein‐synthesis inhibitory protein from seeds of Luffa cylindria roem
Author(s) -
Kishida Kazuo,
Masuho Yasuhiko,
Hara Takeshi
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80149-5
Subject(s) - reticulocyte , sephadex , ribosome inactivating protein , lysis , chemistry , ricin , biochemistry , fractionation , ammonium sulfate , chromatography , cytotoxicity , protein biosynthesis , microbiology and biotechnology , phosphate , biology , ribosome , enzyme , toxin , messenger rna , in vitro , rna , gene
A protein (designated as luffin) with an app. M r of 26000, which inhibits protein synthesis in rabbit reticulocyte lysate, was purified to homogeneity from the seeds of Luffa cylindria roem by extraction with 20 mM Na phosphate buffer (pH 7.2) containing 0.2 M NaCl, ammonium sulfate fractionation, and chromatography on Sephacryl S‐200 and CM‐Sephadex C‐25. Luffin exhibited 10‐times as strong inhibitory activity against protein synthesis in rabbit reticulocyte lysate ( IC 50 , 0.42 ng/ml) as that of ricin A‐chain, but it showed only a weak cytotoxicity against murine leukemia L1210 cells, an activity of 1/10 6 to 1/10 5 that of ricin.