Plant Physiol. Journal of Pharmacology and Experimental Therapeutics
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Plant Physiology 95:286-290 (1991)
© 1991 American Society of Plant Biologists

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Cellular and Structural Biology

Antigenic and Calcium Binding Properties of a Peptide Containing the Essential Cysteine in Lima Bean Lectin 1

Mary J. Maliarik, David D. Roberts2 and Irwin J. Goldstein

Department of Biological Chemistry, The University of Michigan, Ann Arbor, Michigan 48109

Polyclonal antisera were raised against a peptide containing the cysteine residue required for carbohydrate binding activity in the lima bean lectin. The antisera were tested for cross-reactivity with (a) synthetic peptide analogs to the essential cysteine containing peptide, (b) proteolytic digests of related lectins, (c) native lectins. The antisera were specifically inhibited from binding to a peptide conjugate by free synthetic peptides. The degree of inhibition by lectin digests correlated approximately along evolutionary relationships and the degree of sequence conservation. One antiserum was found to cross-react with certain lectins in the native state. In a second set of experiments, the calcium binding properties of the synthetic peptides were investigated using metal ion-chelate chromatography and UV-difference spectroscopy. The nonapeptide and undecapeptide bound to a Ca2+ iminodiacetic acid agarose column and were eluted with EDTA. Ultraviolet difference spectral titrations with Ca2+ performed on the synthetic undecapeptide and a related favin derived peptide resulted in dissociation constants of approximately 6 x 103 per molar.

2 Present address: Laboratory of Pathology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892.

1 This research was supported by National Institutes of Health grant GM 29470.






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Copyright © 1991 by the American Society of Plant Biologists