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Isolation and partial characterization of a novel and uncommon two-chain 64-kDa ribosome-inactivating protein from the bark of elder (Sambucus nigra L.)



Isolation and partial characterization of a novel and uncommon two-chain 64-kDa ribosome-inactivating protein from the bark of elder (Sambucus nigra L.)



FEBS Letters 413(1): 85-91



A novel, strongly basic, two-chain ribosome-inactivating protein (RIP) with an apparent Mr of 64000 by SDS-PAGE and 63469 by mass spectrometry analysis, that we have named basic nigrin b, has been found in the bark of elder (Sambucus nigra L.). The new protein does not agglutinate red blood cells, even at high concentrations and displays an unusually and extremely high activity towards animal ribosomes (IC50 of 18 pg/ml for translation by rabbit reticulocyte lysates). However, it is inactive against plant and HeLa cells protein synthesis. Our functional and structural data are consistent with a heterodimeric structure for basic nigrin b of the type A-B*, B* being a truncated lectin lacking functional binding domains equivalent to the B (lectin) chain of the type 2 RIP SNA I and nigrin b present also in elder bark.

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Accession: 003185245

Download citation: RISBibTeXText

PMID: 9287122

DOI: 10.1016/s0014-5793(97)00882-x


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