Albumins are readily soluble in water and can only be precipitated by high concentrations of neutral salts such as ammonium sulfate. The solution stability of albumin is very good (especially if the solutions are stored aliquoted and frozen). Albumin is readily coagulated by heat. When heated to 50 °C or above, albumin quite rapidly forms hydrophobic aggregates which do not revert to monomers upon cooling.
- Fatty Acids: ≤0.24 mg/g
- Moisture: ≤5%
Albumins are a group of acidic proteins which occur in the body fluids and tissues of mammals and in some plant seeds. Serum and plasma albumin is carbohydrate free and comprises 55-62% of the protein present. Bovine albumin is a single polypeptide chain consisting of approximately 583 to 595 amino acid residues and no carbohydrates. At pH 5-7 it contains 17 intra-chain disulfide bridges and 1 sulfhydryl group. Additional removal of impurities can be accomplished by crystallization, preparative electrophoresis, ion exchange chromatography, affinity chromatography (e.g., ConA-agarose removes glycoproteins), heat treatment (removes globulins), low pH treatment, charcoal treatment, organic solvent precipitation (i.e. isooctane) and low temperature treatment. Charcoal treatment and organic solvent precipitation remove fatty acids.
A fatty acid free bovine albumin powder designed for the most sensitive research and diagnostic applications. Manufactured by a process specifically designed to give consistently low levels of residual metabolites and enzymes. Especially suitable for RIA and enzyme kits as a protein base. Albumin binds water, Ca2+, Na+ and K+. Due to a hydrophobic cleft, albumin binds fatty acids, bilirubin, hormones and drugs. The main biological function of albumin is to regulate the colloidal osmotic pressure of blood and to a lesser degree to provide cellular nutrition. Human and bovine albumins contain 16% nitrogen and are often used as standards in protein calibration studies. Albumin is used to solubilize lipids, stabilize protein solutions, and is also used as a blocking agent in Western blots or ELISA applications. Globulin free albumins are suitable for use in applications where no other proteins should be present such as electrophoresis. Insulin RIA: 1 micro unit/gm T3 and T4 at or below detectable levels.
Certain conformational and primary-sequence epitopes of BSA are suspected allergens in human beef and milk allergies.
