Abstract
An abnormal isozyme of alkaline phosphatase (ALP: orthophosphoric monoester phosphohydrolase, EC 3. 1. 3. 1) detected in the serum of four children with no malignancy is described.The molecular weights of the abnormal enzyme in all four patients were about 1.7×105 daltons, and the enzyme migrated to the front position of the liver ALP (α1∼α2 globulin region) irrespective of electrophoretic medium. Other features of the enzyme, i.e., Michaelis constants, molecular sizes, susceptibilities to amino acids and to the action of neuraminidase, and heat stability suggest that this enzyme is an anomalous bone ALP with respect to sugar chains.
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