Properties of casein, BSA, and lysozyme

Range Table - link
Organism Generic
Reference Pim van Hee, Selective recovery of micrometer bioparticles using aggregation and air flotation, thesis, 2006, Department of Biotechnology, Delft University of Technology The netherlands (downloadable for free from the internet) p. 110 table 5.1
Primary Source List of references under table
Method For Casein: surface plasmon resonance (SPR). For BSA, (Ikeda et al., 2000): BSA solutions were prepared by dissolving in distilled water, with/ without 0.1 mol/dm3 alkali metal salts, under moderate stirring for 90 min. Solutions containing 1-10% w/w BSA showed pH values of ca. 7.0. The volume fraction F, of BSA, was determined spectrophotometrically at 279 nm (UV-2500PC, Shimadzu, Kyoto, Japan) using the extinction coefficient e279=0.667 cm^2/mg, and the partial specific volume=0.734. BSA is an R-helix rich protein and is an elongated ellipsoid, in shape, with semiaxes of ca. 7 and 2 nm, while Stoke’s radius has been determined to be 3.48 nm.
Comments Radii of casein (Stoke's radius, BNID 103862), BSA (Stoke's radius BNID 105488), and lysozyme, are respectively 2.9-3.7, 3.48, and 1.8 nm. See BNID 101827
Entered by Uri M
ID 103880