Metal ion induced conformational changes in concanavalin A: Evidence for saccharide binding to one metal free structure

C. A. Stark, A. D. Sherry

Research output: Contribution to journalArticle

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Abstract

The addition of Mn2+, Zn2+, Co2+, Ca2+ or Pb2+ to apo-concanavalin A results in a slow conformational conversion of the protein to the active saccharide binding form. The rates of conversion are dependent upon the sample pH and identity of the ions which occupy the native transition metal and calcium ion sites yet the affinity of each metalloform for the fluorescent sugar, 4-methylumbelliferyl-α-D-mannopyranoside, is independent of these same parameters (above pH 5.6). EDTA quickly removes all metal ions from the active Mn2+ or Co2+-concanavalin A samples leaving a metastable metal free structure which retains its high saccharide affinity for several hours at room temperature. This form of apo-concanavalin A and the metallized derivatives have equally high saccharide binding affinities in 1M NaCL but the former dramatically loses its sugar affinity as the ionic strength is lowered.

Original languageEnglish (US)
Pages (from-to)598-604
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume87
Issue number2
DOIs
StatePublished - Mar 30 1979

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ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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