PMID: 9540803Apr 16, 1998Paper

Novel lectin-related proteins are major components in lima bean (Phaseolus lunatus L.) seeds

Biochimica Et Biophysica Acta
F SparvoliR Bollini

Abstract

The only component of the lectin-related protein family so far reported in Lima bean (Phaseolus lunatus L.) seeds is the minor seed lectin (LBL). In the morphotype Big Lima, we have isolated and characterised two abundant lectin-related seed proteins and the corresponding cDNA clones. The clones show 93.7% nucleotide identity and encode an arcelin-like (ARL) and an alpha-amylase inhibitor-like (AIL) protein. Not considering the signal peptides, ARL and AIL polypeptides contain 239 and 233 amino acids, respectively. Each polypeptide is present in the mature protein as two glycoforms. ARL subunits (43 and 46 kDa) make up oligomers of about 125 to 130 kDa whereas AIL subunits (40 and 42 kDa) oligomerise in dimers of about 88 to 100 kDa. cDNA clones encoding two isoforms of the less abundant Lima bean lectin were also isolated. In common bean (P. vulgaris) the lectin locus encodes the lectin and the lectin-related proteins alpha-amylase inhibitor and arcelin, all plant defence proteins. Our data indicate extensive evolution of the locus also in Lima bean.

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Citations

Aug 19, 2007·TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik·L LioiF Sparvoli
Jan 3, 2001·The Plant Journal : for Cell and Molecular Biology·F SparvoliR Bollini
Mar 16, 2012·Journal of the Science of Food and Agriculture·Angela R PiergiovanniMassimo Zaccardelli
Apr 7, 2004·TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik·I GalassoF Sparvoli

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