BSA结构.docVIP

INTERACTION OF SWP WITH BOVINE SERUM ALBUMIN (BSA) Introduction Serum albumin is one of the most widely studied proteins and is the most abundant protein in plasma with a typical concentration of 5g/100ml. Various researchers have studied the structure and properties of serum albumin and its interaction with other proteins in order to understand how serum albumin affects the functionality of foods in which they have been included as well as novel applications. The latter reason led to the study of the interaction between soluble wheat protein and bovine serum albumin. The structure and properties of SWP are described in chapters 2, 3 and 4. The following sections describe the structure and properties of BSA. Bovine serum albumin (BSA) Albumin is generally regarded to mean serum albumin or plasma albumin (care should be taken to distinguish albumen, which refers to egg white, from albumin or serum albumin). The word albumin is also used to describe a protein or a group of proteins defined by solubility in water for example the albumin fraction of wheat (chapter 2). Albumin is the most abundant protein in the circulatory system and contributes 80% to colloid osmotic blood pressure (Carter and Ho, 1994). It has now been determined that serum albumin is chiefly responsible for the maintenance of blood pH (Figge et al., 1991). In mammals albumin is synthesized initially as preproalbumin by the liver. After removal of the signal peptide, the resultant proalbumin is further processed by removal of the six-residue propeptide from the new N-terminus. The albumin released into circulation possesses a half-life of 19 days (Waldmann, 1977). Structure of BSA The substantial information on serum albumin has led to some contradictory results and discussions. Based largely on hydrodynamic experiments (Hughes, 1954; Squire et al., 1968; Wright and Thompson, 1975) and low-angle X-ray scattering (Bloomfield, 1966), serum albumin was postulated to be an oblate ellipsoid with dimen