Study of interaction between catechin and native and modified bovine serum albumin by physico-chemical methods.
The interaction of native and modified bovine serum albumin (BSA) with catechin, a flavanoid having vitamin P activity, has been studied using equilibrium dialysis, pH-metric, viscosity and spectrophotometric methods. The order of reactivity of catechin binding to proteins was found to be: esterified BSA greater than BSA greater than formylated BSA greater than acetylated BSA with log K values of 3.778, 3.879, 3.748 and 3.813 and free energy change equal to -5.11, -5.16, -5.07 and -5.15 kcal/mole, respectively.
J P
JP
Arora
V K
VK
Singhal
M
M
Chand
Laxmi
C
C
Pal
D002392:Catechin / Q000378:metabolism*; D003956:Dialysis; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000378:metabolism*; D013053:Spectrophotometry; D014783:Viscosity
D012710:Serum Albumin, Bovine; D002392:Catechin