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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.)
Author(s) -
de Benito Fernando M.,
Citores Lucı́a,
Iglesias Rosario,
Ferreras J.Miguel,
Camafeita Emilio,
Méndez Enrique,
Girbés Tomás
Publication year - 1997
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/s0014-5793(97)00882-x
Subject(s) - sambucus nigra , bark (sound) , isolation (microbiology) , chemistry , botany , biochemistry , traditional medicine , biology , medicine , lectin , microbiology and biotechnology , ecology
A novel, strongly basic, two‐chain ribosome‐inactivating protein (RIP) with an apparent M r of 64 000 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 (IC 50 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.