Electrochemical potential of Microgramma vaccinifolia rhizome lectin

Bioelectrochemistry. 2012 Jun:85:56-60. doi: 10.1016/j.bioelechem.2011.11.006. Epub 2011 Dec 6.

Abstract

This work reports the isolation of Microgramma vaccinifolia rhizome lectin (MvRL) and the determination of electrochemical potentials of MvRL in the presence of Ca²⁺, Mg²⁺ and human type O erythrocytes. MvRL showed the highest specific hemagglutinating activity with human type O erythrocytes and showed a single polypeptide band of 17 kDa on SDS-PAGE. MvRL hemagglutinating activity was neutralized after dialysis with EDTA, and addition of Ca²⁺ and Mg²⁺ restored the activity. Electrochemical potentials of MvRL in the presence of 100 mM Ca²⁺ (882 mV) and 60 mM Mg²⁺ (1051 mV) were higher (p<0.05) than in the presence of only 0.15 M NaCl (247 mV), indicating that the electrochemical system was sensitive to structural and physico-chemical changes promoted by these ions. MvRL potential did not change in the presence of type O erythrocytes. The electrochemical system was able to detect changes in electrochemical potentials of MvRL promoted by Ca²⁺ and Mg²⁺, even in a complex environment (human serum supplemented with 40 and 60mM of these ions). The study reveals that the stimulatory effect of Ca²⁺ and Mg²⁺ on hemagglutinating activity may be linked to conformational change and/or alterations in surface charge distribution of MvRL.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Calcium
  • Electrochemistry / methods*
  • Erythrocytes
  • Hemagglutination
  • Humans
  • Lectins / chemistry*
  • Lectins / isolation & purification
  • Magnesium
  • Protein Conformation
  • Rhizome / chemistry*

Substances

  • Lectins
  • Magnesium
  • Calcium