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The organ-specificity of animal alkaline phosphatases and the origin of alkaline phosphatase in human serum in hyperphosphatasemias

The organ-specificity of animal alkaline phosphatases and the origin of alkaline phosphatase in human serum in hyperphosphatasemias

Biochim Et Biophys Acta 5(2): 275-284

The affinity of alkaline phosphatases (phosphomonoesterases) (I) of various animal tissues for Na beta-glycerophosphate was studied at pH 9.4 and 37[degree]. Under the conditions of the expts., the value of the affinity constant KM was very different for the I of bone, intestine, kidney and liver. Thus the I of these organs were not identical. Human blood serum contained at least two I; the level of one alone increased in the hyperphosphatasemias. Nearly all of these corresponed to the presence of an excess of liver (I) an excess of bone enzyme being exceptional. It was possible that modifications of the affinity of the last one were due to certain bone disease.

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