English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

The binding of mercury (II) ion has been studied with egg protein at different pH values and temperatures by the polarographic technique. The binding data were found to be pH and temperature dependent. The intrinsic association constants (k) and the number of binding sites (n) were calculated from Scatchard plots and found tobe at the maximum at lower pH and at lower temperatures. The free energy change (ΔG°) of the combining sites were least at the higher pH and highest at the low pH; therefore, a lower temperature and lower pH offered more sites in the protein molecule for interaction with mercury (II) ions. Statistical effects seem to be more significant at lower mercury (II) ion concentrations, while at higher concentrations electrostatic effects and heterogeneity of sites are more significant.

The Thermodynamic and Binding Studies of Hg +2 Ions with Egg Protein by Polarographic and pH Metric Techniques