Studies on a Phytohemagglutinin from the Lentil

作者：Irmgard Keeler Howard, Harvey J. Sage, Marshall D. Stein, Noel Martin Young, Myron A. Leon, Douglas F. Dyckes · 发表于：Journal of Biological Chemistry · 年份：1971 · DOI：10.1016/s0021-9258(18)62353-1 · 被引用次数：203 · 研究领域：Legume Nitrogen Fixing Symbiosis、Botanical Research and Chemistry、Agricultural pest management studies

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.