||Cow Bos Taurus
||Shinya Ikeda and Katsuyoshi Nishinari, Intermolecular Forces in Bovine Serum Albumin Solutions Exhibiting Solidlike Mechanical Behaviors, Biomacromolecules 2000, 1, 757-763 DOI: 10.1021/bm005587o p.759 left column 3rd paragraphPubMed ID11710208
|| Axelsson, I. J. Characterization of proteins and other macromolecules by agarose gel chromatography, Chromatogr. 1978, 152, 21-32. link
||P.759 left column 3rd paragraph: "Cold alcohol precipitated BSA was purchased from Sigma Chemicals (St. Louis, MO) and used without further purification. Other chemicals were of reagent grade quality. BSA solutions were prepared by dissolving in distilled water, with/without 0.1 mol/dm^3 alkali metal salts, under moderate stirring for 90 min. Solutions containing 1−10% w/w BSA showed pH values of ca. 7.0. Some solutions were titrated with 0.1 mol/dm^3 HCl, or acetic acid, to be pH = 4.5. The volume fraction φ, of BSA, was determined spectrophotometrically at 279 nm (UV-2500PC, Shimadzu, Kyoto, Japan) using the extinction coefficient ε279 = 0.667 cm^2/mg (ref 41), and the partial specific volume υ = 0.734 (ref 42) BSA is an α-helix-rich protein (ref 43) and is an elongated ellipsoid, in shape, with semiaxes of ca. 7 and 2 nm (ref 44) while Stoke's radius has been determined to be 3.48 nm (primary source)."
||Note-estimated hydrated BSA radius of 3.2nm given in Yaoqi 1998 p. 10619 table 1 (for full reference see BNID 103737). See BNID 101827