Studies on alkaline phosphatase. Phosphorylation of calf intestinal alkaline phosphatase by 32P-labelled pyrophosphate
Keyword(s):
1. A purified preparation of alkaline phosphatase from calf-intestinal mucosa was phosphorylated by 32P-labelled PPi at a serine residue on the enzyme. Under the conditions employed, up to 0·15μm-labelled sites were obtained from 1μm-[32P]PPi. 2. The phosphorylated enzyme was labile, the rate of dephosphorylation being similar to the overall rate of substrate hydrolysis. 3. A stopped-flow technique was used to determine the number of phosphomonoesterase active sites, which agreed with the number of 32P-labelled sites. 4. It is concluded that calf-intestinal alkaline phosphatase is both a phosphomonoesterase and a pyrophosphatase.
1955 ◽
Vol 33
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pp. 89-92
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1998 ◽
pp. 47-52
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2003 ◽
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pp. 737-744
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1982 ◽
Vol 65
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pp. 2668-2681
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pp. 1241-1247
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1954 ◽
Vol 32
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pp. 621-624
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