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. 1966 Nov;101(2):460-6.
doi: 10.1042/bj1010460.

The catalytic-centre activity and kinetic properties of bovine milk alkaline phosphatase

T E Barman, H Gutfreund

The catalytic-centre activity and kinetic properties of bovine milk alkaline phosphatase

T E Barman et al. Biochem J. 1966 Nov.

Abstract

1. The phosphorylation of milk alkaline phosphatase was studied under various conditions: maximum incorporation occurred at pH5.0 and 50% incorporation at pH6.6-7.0. 2. The phosphorylation was shown to be specific and the results suggest that the active centre of the enzyme is involved in the process. 3. Phosphoryl-enzyme is rapidly hydrolysed at alkaline pH. at pH7.0 the results suggest that a phosphoryl-enzyme could occur as a transient intermediate in the hydrolysis of phosphate esters by the phosphatase. 4. The catalytic-centre activity of the enzyme was found to be 2700sec.(-1) at pH10.0 and 25 degrees with p-nitrophenyl phosphate as substrate.

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