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The Studies of Density, Apparent Molar Volume, and Viscosity of Bovine Serum Albumin, Egg Albumin, and Lysozyme in Aqueous and RbI, CsI, and DTAB Aqueous Solutions at 303.15 K
Author(s) -
Singh Man,
Chand Hema,
Gupta K. C.
Publication year - 2005
Publication title -
chemistry and biodiversity
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.427
H-Index - 70
eISSN - 1612-1880
pISSN - 1612-1872
DOI - 10.1002/cbdv.200590059
Subject(s) - chemistry , lysozyme , bovine serum albumin , aqueous solution , chromatography , albumin , viscosity , egg albumin , molar , molar volume , serum albumin , denaturation (fissile materials) , ammonium bromide , intermolecular force , salt (chemistry) , bromide , crystallography , nuclear chemistry , molecule , organic chemistry , biochemistry , thermodynamics , pulmonary surfactant , medicine , physics , dentistry
Density ( ρ ), apparent molar volume ( V ϕ ), and viscosity ( η ) of 0.0010 to 0.0018% ( w / v ) of bovine serum albumin (BSA), egg albumin, and lysozyme in 0.0002, 0.0004, and 0.0008 M aqueous RbI and CsI, and (dodecyl)(trimethyl)ammonium bromide (DTAB) solutions were obtained. The experimental data were regressed against composition, and constants are used to elucidate the conformational changes in protein molecules. With salt concentration, the density of proteins is found to decrease, and the order of the effect of additives on density is observed as CsI>RbI>DTAB. The trend of apparent molar volume of proteins is found as BSA>egg‐albumin>lysozyme for three additives. In general, η values of BSA remain higher for all compositions of RbI than that of egg‐albumin for CsI and DTAB. These orders of the data indicate the strength of intermolecular forces between proteins and salts, and are helpful for understanding the denaturation of proteins.