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Purification and Partial Characterization of a Lectin from Phaseolus vulgaris
Author(s) -
Renato de Azevedo Moreira,
J. C. PERRONE
Publication year - 1977
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.59.5.783
Subject(s) - phaseolus , isoelectric point , isoelectric focusing , chromatography , chemistry , lectin , biochemistry , amino acid , histidine , phytohemagglutinins , biology , botany , enzyme , immune system , t cell , lymphocyte activation , immunology
A method is presented for the isolation of a lectin from a Brazilian cultivar of the common bean (Phaseolus vulgaris L.), through extraction in acidic (pH 4.2) medium, fractionation with ammonium sulfate, and chromatography on DEAE-cellulose. The lectin was shown to be homogeneous by gel electrophoresis and isoelectric focusing.The molecular weight, determined by osmometry, is 100,250 daltons; the isoelectric point, determined by isoelectric focusing, is pH 5.1; and the extinction coefficient at 280 nm and pH 7 is E(1%) (1 cm) = 7.85.The lectin was shown to be a glycoprotein with 9.11% of neutral sugars and 1.44% of amino sugars. Its amino acid composition was characterized by the absence of methionine and a very low content of half-cystine, with a predominance of acidic and hydroxylated amino acids.The lectin presented no specificity when tested with red blood cells of all the groups of the ABO system.

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