Interaction of Tetra-iodophenolsulphonphthalein with Proteins

Abstract

The formation of microelectrostatic fields in proteins is proposed and
it causes the aggregation of stain. We have studied the interaction of
tetra-iodophenolsulphonphthalein (TIPST) with two proteins: bovine
serum albumin (BSA), ovalbumin (OVA) and Iysoxyme (LYS). Results
showed that the adsorption ratios of BSA, OVA and LYS are 10.5-8.00,
0.72-0 .64 and 0.81-0.64, respectively and their adsorption constants
K_BSA-TIPST = 3.34 x 10⁵-2.18 x 10⁵,  K_OVA-TIPST = 1.50 x 10⁵- 1.05 x 10⁵
and K_LYS-TIPST = 3.25 x 10⁴-5.34 x 10⁴ . and their absorptivities
2.48 x 10⁵-2.29 x 10⁵,  2.32 x 10⁴-2.16 x 10⁴  and 4.55 x 10⁴-3.79 x 10⁴
L mole^-1  cm^-1 at 628 nm.