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Gāndhī Nagar, India

Singh R.P.,Sanjay Gandhi Postgraduate College | Singh R.P.,DAV College Kanpur | Gupta D.,Sanjay Gandhi Postgraduate College
Asian Journal of Chemistry | Year: 2010

This paper reports the synthesis of Mn(II), Fe(II) and cochelates derived from 2,6-diacetyl pyridine dihydrazide and diacetyl with the general composition [M(C 13H 15N 5)X 2] where, M = Mn 2+, Fe 2+, Co 2+ and X = Cl, Br, NO 3 or NCS. All the chelates were characterized by elemental analysis, molar conductance, magnetic susceptibility measurements, electronic and IR spectral studies. On the basis of these studies, the divalent metal complexes have been assigned trigonal bipyramidal geometry with high spin. Source


Singh R.P.,Sanjay Gandhi Postgraduate College | Singh R.P.,DAV College Kanpur | Chaudhary R.,Sanjay Gandhi Postgraduate College | Chaudhary R.,DAV College Kanpur | And 5 more authors.
Asian Journal of Chemistry | Year: 2010

The binding of molybdenum with trypsin and pepsin enzymes has been studied using dialysis equilibrium technique. The effect of pH and temperature on the anion binding behaviour has been explained in the light of protonation and deprotonation behaviour of the two enzymes. The differences in binding behaviour has been attributed to large differences in their cationic groups contents. The binding constants, viz. intrinsic association constants (K) and binding sites (n) were determined from Scatchard's plots. The linear nature of plots under similar conditions of pH and temperature in two cases is an indication of the involvement of a single one class of sites. The pH dependence of anion binding exhibited the involvement of cationic groups in the interaction. The nearly similar values of free energy and entropy changes for trypsin and pepsin is an index of their similar anion binding capacity. The enthalpy and entropy changes at pH 5.50 provided evidence for covalent linking between molybdenum and enzyme groups. Source


Singh R.P.,Sanjay Gandhi Postgraduate College | Singh R.P.,DAV College Kanpur | Rani R.,Sanjay Gandhi Postgraduate College | Kumar S.,Sanjay Gandhi Postgraduate College | And 3 more authors.
Asian Journal of Chemistry | Year: 2010

The binding of hydrous oxide sols of aluminium, iron and chromium with pepsin was studied by pH-metric method. The shifts in the titration curves was used as a means to explain the interaction of metals in the hydrous oxide sols with the various ionizable groups of pepsin. The interaction of chromium and aluminium is assumed to take place through the carboxyl groups of pepsin, since the flat segment of the pepsin sol curve lies between pH 3.0 to 6.0 where the carboxyl groups are deprotonated. The similar segment of iron oxide sol-pepsin curve lies in the acid range. Hence, the interaction could not be expected with carboxyl groups, but the phenolic groups of tyrosine may be involved in the binding interaction. The quantitative calculation revealed higher binding in low pH than in higher pH which is in accordance that pepsin contained larger anionic carboxylic groups than basic groups. The order of linking is acidic and basic ranges were identified. Source

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