Purification and Characterization of Alkaline Phosphatase from Rat Kidney
1976 Volume 79 Issue 2 Pages 283-288
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1976 Volume 79 Issue 2 Pages 283-288
Alkaline phosphatase [EC 3.1.3.1] was purified about 250-fold from rat kidney, and its enzymological properties were studied.
Kidney homogenate was extracted with n-butanol, passed through Sephadex G-200 and chromatographed on a DEAE-cellulose column. The peak from the DEAE-cellulose column was subjected to isoelectric focusing, and the alkaline phosphatase activity was separated into two peaks. The molecular weights of alkaline phosphatase in these peaks were 4.8×104 and 1.0×105, as determined by SDS-polyacryl-amide gel electrophoresis.
Anti-serum against alkaline phosphatase from rat kidney was prepared, and was shown to neutralize the activity from kidney, liver or bone, but not that from intestine.
