Abstract
FISHMAN et al. reported that human placental alkaline phosphatase (Regan isoenzyme) was found in the serum and tumour tissue of a patient with lung cancer1. Two electrophoretically different variant forms of Regan alkaline phosphatase with a greater sensitivity to inhibition by L-leucine have since been described: the ‘Nagao isoenzyme’2, and a hepatoma-specific alkaline phosphatase3–5. Inglis et al.6 reported that the L-leucine-sensitive Nagao isoenzyme found in some cancer patients closely resembled the ‘D variant’ of human placental alkaline phosphatase, a rare phenotype defined electrophoretically on starch gel which is found in less than 1% of the general population of pregnancies7. An example was reported of a pregnancy serum D-phenotype enzyme presumably of placental origin, confirmed by electrophoresis established as L-leucine-sensitive6. Most interesting was the occurrence of the variant at high frequency in the ovarian cancer patients surveyed6,8. To extend the observations of Inglis et aL, screening for the phosphatases in placentae was carried out, both to establish the frequency of the L-leucine-sensitive placental phenotypes (which should match the frequency of the electrophoretically defined D variant phenotypes) and to provide enough enzyme to enable purification and characterisation. Supply of cancer tissue is generally restrictive for this purpose.
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References
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DOELLGAST, G., FISHMAN, W. L-leucine, a specific inhibitor of a rare human placental alkaline phosphatase phenotype. Nature 259, 49–51 (1976). https://doi.org/10.1038/259049a0
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DOI: https://doi.org/10.1038/259049a0
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