Publication | Open Access
Studies on a Phytohemagglutinin from the Lentil
202
Citations
53
References
1971
Year
GlycosylationBiochemistryTanninNatural SciencesMedicineProteomicsGlycobiologyBioanalysisMolecular BiologyCommon Primary SequencePeptide LibraryPhytopharmacologyUnique SequenceCarbohydrate-protein InteractionPharmacologyL. Culinaris BProtein Purification
Two electrophoretically distinguishable hemagglutinins, Lens culinaris A (LcH-A) and L. culinaris B (LcH-B), have been obtained from the common lentil L. culinaris in homogeneous forms. Each protein had a molecular weight of 49,000, and each consisted of two identical polypeptide chains of 24,500 molecular weight. The proteins were immunochemically indistinguishable and had identical hemagglutinin activity and very similar compositions. LcH-B contained 4 more lysine residues per molecule than LcH-A, accounting for their different electrophoretic properties. Peptide mapping indicated that both proteins have a large majority of common primary sequence with small areas of unique sequence. Individual lentil seeds all contained both LcH-A and LcH-B, but with varying proportions depending on the source of the lentils.
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