Improved purification of rat intestinal lactase.
A rapid and improved method to obtain purified lactase from rat intestine is described. The purification procedure involved only two chromatographic steps. The degree of purification was far above (500 fold) the values reached with classical methods. Rabbit antisera raised to the purified lactase were characterized using conventional immunological techniques. The specificity of the lactase antibodies was confirmed by the lack of interference on maltase, aminopeptidase and alkaline phosphatase activities measured after papain extraction of the membrane proteins.
D000818:Animals; D000918:Antibody Specificity; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D005696:Galactosidases / Q000302:isolation & purification*; D007124:Immunoenzyme Techniques; D007421:Intestine, Small / Q000201:enzymology* / Q000648:ultrastructure; D008871:Microvilli / Q000032:analysis / Q000201:enzymology; D051381:Rats; D011919:Rats, Inbred Strains; D011947:Receptors, Antigen, B-Cell / Q000276:immunology; D001616:beta-Galactosidase / Q000302:isolation & purification*
D011947:Receptors, Antigen, B-Cell; D005696:Galactosidases; D001616:beta-Galactosidase