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Purification and partial characterization of two lectins fromMomordica charantia

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Summary

2 different lectins have been purified from the seeds ofMomordica charantia by gel-filtration and ion-exchange chromatography. These 2 lectins appear to be composed of 2 subunits of 26,000 daltons. Protein fraction I, but not II, showed agglutinating activity toward human type-O red blood cells. The amino acid compositions and amino-terminal sequences of these two homologous proteins are quite different.

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Authors and Affiliations

  1. Department of Microbiology, Mount Sinai School of Medicine, 10029, New York, New York, USA

    S. S. -L. Li

  2. Laboratory of Environmental Mutagenesis, NIEHS, NIH Research, 27709, Triangle Park, North Carolina, USA

    S. S. -L. Li

Authors
  1. S. S. -L. Li
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Acknowledgment. The skillful assistance of Ms M. Diane Forde is greatly acknowledged. Part of this work was supported by NIH grants CA18621 and AI09810 when the author was at Mount Sinai School of Medicine.

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Li, S.S.L. Purification and partial characterization of two lectins fromMomordica charantia. Experientia 36, 524–527 (1980). https://doi.org/10.1007/BF01965777

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