This research work is based on the studies on the binding of
soluble ovalbumin, transfusion gelatin, -amylase proteins with
vanadium and molybdenum etc. applying various physico-chemical
methods such as pH-metery, dialysis equilibrium, spectrophotometry,
polarography etc. The work also includes the binding of metal
hydrous oxide sols to these proteins. The effect of anionic
surfactants like triethanolamine lauryl sulphate, sodium dodecyl
benzene sulphonate was also studied on ovalbumin casein and
-amylase by viscometric and other related methods. The binding
results are helpful in proposing a mechanism of ligand interaction
with biopolymers in livings mediated by metal ions. The additions
of proteins may decrease the critical micelle concentrations of the
surfactants. This aspect possesses a good means of increasing the
detergency of the surfactants.
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