Fractionation of Milk Proteins on Anion-Exchange Cellulose

The fractionation of urine colloids on anion-exchange cellulose.

Human gamma globulin fractionation on anion exchange cellulose columns.

The serum proteins designated as y-globulins include all proteins of the slowest moving of the several major protein groups seen on serum electrophoresis conducted at alkaline pH (2). Among the y-globulins of normal serum are proteins of differing electrophoretic mobility (3,4), proteins with sedimentation coefficients of 6.6 S and 18 S in the ultracentrifuge (2, 3, 5, 6)) many individual antib...

Fractionation of milk proteins.

No group of proteins has been as extensively investigated or as well characterized as bovine milk proteins. This can be attributed not only to the importance of milk as a food and as a raw material for a vast processing industry, but also to its convenience as an abundant source of relatively pure protein of varied structure and properties. In spite of the vast range of information available, h...

Fractionation of the major whey proteins and isolation of b-Lactoglobulin variants by anion exchange chromatography

A method for the separation and fractionation of the major whey proteins from a whey protein concentrate (WPC80) by anion-exchange chromatography coupled to a Fast Protein Liquid Chromatography (FPLC) system is proposed. The method is based on the use of an ionic column (Mono Q) and a salt gradient elution by increasing the ionic strength of the elution buffer (Tris–HCl 20 mM plus 0 to 1 M NaCl...

Thyroglobulin fractionation on diethylaminoethyl cellulose columns.

Thyroglobulin may be defined as the iodine-containing protein of the thyroid gland which has a sedimentation coefficient of 4o.w = 19 S, an electrophoretic mobility at pH 8.6 of approximately 5 x 10F5 cm2 volt-l set-1, and a steep salting out curve at about 38% ammonium sulfate saturation at neutral pH (1). Although other iodoproteins, both soluble in neutral salt and attached to cell particles...