title: Purification and characterization of four components of rat caseins.
abstract: Rat casein components (C1-, C3A-, C3B- and C4-casein) were extensively purified from rat milk, and the properties of these proteins were compared with those of other caseins including rat C2-casein. C1-casein was precipitated by a low concentration of CaCl2 (1.5 mM). Both C3A- and C3B-casein were less sensitive to Ca2+ than were C1- and C2-casein, and the presence of 20 mM CaCl2 was required at 37 degrees C for their precipitation. C4-casein was absolutely insensitive to Ca2+. This protein exhibited the ability to stabilize all of the other rat casein components against Ca2+-dependent precipitation. In addition, C4-casein contained sialic acid, galactose and N-acetylgalactosamine. Therefore, C4-casein appears to be a bovine kappa-casein-like protein.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002118:Calcium / Q000494:pharmacology; D002364:Caseins / Q000302:isolation & purification*; D002846:Chromatography, Affinity; D002848:Chromatography, DEAE-Cellulose; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D008892:Milk / Q000032:analysis; D008970:Molecular Weight; D009904:Optical Rotation; D051381:Rats
chemical_list: D000596:Amino Acids; D002364:Caseins; D002118:Calcium