The isolation and properties of the dimeric subunit of Concanavalin A

John H. Pazur, Michael D. Perloff, Adam R. Frymoyer, Carolyn J.P. Jensen, Holly Micolochick, Andrea Mastro

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2 Scopus citations

Abstract

Concanavalin A (Con A) was dissociated into dimeric and monomeric subunits by incubation at 37°C in acetate buffer of pH 3.8 containing 0.5% sodium dodecyl sulfate. The dimer was isolated in pure form by a density gradient ultracentrifugation method. Several properties of the dimer were determined including the formation of a precipitin with anti-Con A antibodies, the molecular weight, the lack of a binding site for glycogen, the lack of mitogenic activity for spleen lymphocytes, and the lack of inhibition by α-methyl D-glucoside. The latter findings differ from results reported by other investigators.

Original languageEnglish (US)
Pages (from-to)353-359
Number of pages7
JournalJournal of Protein Chemistry
Volume19
Issue number5
DOIs
StatePublished - Dec 1 2000

All Science Journal Classification (ASJC) codes

  • Biochemistry

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    Pazur, J. H., Perloff, M. D., Frymoyer, A. R., Jensen, C. J. P., Micolochick, H., & Mastro, A. (2000). The isolation and properties of the dimeric subunit of Concanavalin A. Journal of Protein Chemistry, 19(5), 353-359. https://doi.org/10.1023/A:1026431329188