Abstract
Platelet alkaline phosphatase from normal subjects and from trisomy 21 Down's syndrome patients was characterized by means of acrylamide gel disc electrophoresis, neuraminidase sensitivity, heat inactivation, l-phenylalanine and l-homoarginine inhibition.The platelet enzyme from normal and mongoloid children showed the same biophysical and biochemical characteristics. The biochemical properties of platelet alkaline phosphatase were compared with those already found for leukocyte alkaline phosphatase. Alkaline phosphatase derived from these two blood cells showed similar properties.These results suggested that within platelets and leukocytes there exists only a single enzyme. The independent variation of platelet and leukocyte alkaline phosphatase activity in Down's syndrome is therefore probably not caused by differences in structural or regulator genes between these blood cells. Cellular differences in genetic and environmental interactions or tissue specific variations in enzyme regulation should be considered.
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