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Plant Physiology 97:204-211 (1991)
© 1991 American Society of Plant Biologists

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Natural Products

Characterization and Comparison of Arcelin Seed Protein Variants from Common Bean 1

Lynn M. Hartweck, Robert D. Vogelzang and Thomas C. Osborn

Department of Agronomy, University of Wisconsin, Madison, Wisconsin 53706

Four variants of arcelin, an insecticidal seed storage protein of bean, Phaseolus vulgaris L., were investigated. Each variant (arcelin-1, -2, -3, and -4) was purified, and solubilities and Mrs were determined. For arcelins-1, -2, and -4, the isoelectric points, hemagglutinating activities, immunological cross-reactivities, and N-terminal amino acid sequences were determined. On the basis of native and denatured Mrs, the variants were classified as being composed of dimer protein (arcelin-2), tetramer protein (arcelins-3 and -4), or both dimer and tetramer proteins (arcelin-1). Although the dimer proteins (arcelins-1d and -2) could be distinguished by Mrs and isoelectric points, they were identical for their first 37 N-terminal amino acids and had similar immunological cross-reactions, and bean lines containing these variants had a DNA restriction fragment in common. The tetramer proteins arcelin-1t and arcelin-4 also could be distinguished from each other based on Mrs and isoelectric points; however, they had similar immunological cross-reactions and they were 77 to 93% identical for N-terminal amino acid composition. The similarities among arcelin variants, phytohemagglutinin, and a bean {alpha}-amylase inhibitor suggest that they are all encoded by related members of a lectin gene family.

1 Support provided by the Graduate School and the College of Agricultural and Life Sciences, University of Wisconsin, Madison, and by the Plant Cell Research Institute, Inc., Dublin, CA.




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Copyright © 1991 by the American Society of Plant Biologists