Neutral maltase/glucoamylase from rabbit renal cortex.
Maltase activity (EC 3.2.1.20) was solubilized from rabbit kidney brush-border membrane by using 1.0% Triton X-100 and purified 230-fold with an overall recovery of 30%. The purification procedure makes use of heat precipitation, chromatography on DE-52 DEAE-cellulose and gel filtration on Sephacryl S-300. Rabbit kidney brush border exhibited glucoamylase activity with a maltase/glucoamylase ratio of 1.5:1 to 2.0:1. During purification the maltase and glucoamylase activities behaved identically. The Mr of the complex is 590,000, and it appears to be composed of eight identical subunits linked by disulphide bridges.
Pereira
B
B
Department of Life Sciences, University of Bombay, India.
Sivakami
S
S
D000818:Animals; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D005087:Glucan 1,4-alpha-Glucosidase / Q000302:isolation & purification* / Q000378:metabolism; D007672:Kidney Cortex / Q000201:enzymology* / Q000648:ultrastructure; D007700:Kinetics; D008871:Microvilli / Q000201:enzymology; D008970:Molecular Weight; D009097:Multienzyme Complexes / Q000302:isolation & purification* / Q000378:metabolism; D011817:Rabbits; D000520:alpha-Glucosidases / Q000302:isolation & purification* / Q000378:metabolism
D009097:Multienzyme Complexes; D000520:alpha-Glucosidases; D005087:Glucan 1,4-alpha-Glucosidase