Feb 1, 1976

Purification and characterization of alkaline phosphatase from rat kidney

Journal of Biochemistry
K Nose

Abstract

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.X10(4) and 1.0X10(5), as determined by SDS-polyacrylamide 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.

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Mentioned in this Paper

Sephadex G 200
Spleen
2-Mercaptoethanol
August Rats
Alkaline Phosphatase Measurement
1-Butanol
Alkaline Phosphatase
Kidney
DEAE-Cellulose
Intestinal Wall Tissue

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