A comparison of solution conformation and hydrodynamic properties of equine, porcine and rabbit serum albumin using viscometric measurements.
This paper presents the results of viscosity determinations on aqueous solutions of equine, porcine and rabbit serum albumin over a wide range of concentrations and at temperatures ranging from 5 degrees C to (42-45) degrees C. The results are compared with human and bovine serum albumin previously studied. Viscosity-temperature dependence is discussed on the basis of the modified Arrhenius formula. The effective specific volume, the activation energy and entropy of viscous flow for all investigated albumins are compared. Viscosity-concentration dependence, in turn, is discussed on the basis of Mooney equation. Based on the assumption that theoretical and experimental values of Simha factor--at high temperature limit--are equal to each other, the hydrodynamic volume of the studied albumins has been calculated. The numerical values of a self-crowding factor were also obtained. At low concentration limit, the numerical values of the intrinsic viscosity and of Huggins coefficient were compared.
Monkos
Karol
K
Department of Biophysics, Silesian Medical Academy, H. Jordana 19, 41-808 Zabrze 8, Poland. monkos@slam.katowice.pl
D000818:Animals; D002417:Cattle; D006736:Horses; D006801:Humans; D011487:Protein Conformation; D011817:Rabbits; D012709:Serum Albumin / Q000737:chemistry*; D013552:Swine; D013696:Temperature; D014783:Viscosity; D014867:Water / Q000737:chemistry
D012709:Serum Albumin; D014867:Water