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Mechanism of action of Mg2+ and Zn2+ on rat placental alkaline phosphatase. I. Studies on the soluble Zn2+ and Mg2+ alkaline phosphatases

Canadian Journal of Biochemistry

Oct 1, 1975

C PetitClercN Brière

PMID: 1142

Abstract

Rat placental alkaline phosphatase (EC 3.1.3.1), a dimer of 135,000 daltons, is strongly activated by Mg2+. However, Zn2+ has to be present on the apoenzyme to obtain this activation. Mg2+ alone is unable to reconstitute functional active sites. Excess Zn2+ which competes for the Mg2+ s...read more

Mentioned in this Paper

Covalent Interaction
Apoenzymes
Phosphoric Monoester Hydrolases
Placenta Specimen
Alkaline Phosphatase Measurement
MUC7 gene
Placenta
Phosphate Measurement
Alkaline Phosphatase
Plasma Protein Binding Capacity
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Mechanism of action of Mg2+ and Zn2+ on rat placental alkaline phosphatase. I. Studies on the soluble Zn2+ and Mg2+ alkaline phosphatases

Canadian Journal of Biochemistry

Oct 1, 1975

C PetitClercN Brière

PMID: 1142

DOI:

Abstract

Rat placental alkaline phosphatase (EC 3.1.3.1), a dimer of 135,000 daltons, is strongly activated by Mg2+. However, Zn2+ has to be present on the apoenzyme to obtain this activation. Mg2+ alone is unable to reconstitute functional active sites. Excess Zn2+ which competes for the Mg2+ s...read more

Mentioned in this Paper

Covalent Interaction
Apoenzymes
Phosphoric Monoester Hydrolases
Placenta Specimen
Alkaline Phosphatase Measurement
MUC7 gene
Placenta
Phosphate Measurement
Alkaline Phosphatase
Plasma Protein Binding Capacity

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