PLACENTA-LIKE ALKALINE-PHOSPHATASES FROM HUMAN OSTEOSARCOMA CELLS

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  • 1 January 1978
    • journal article
    • research article
    • Vol. 38  (1) , 193-198
Abstract
Hormone-induced alkaline phosphatases in human osteosarcoma cells (LM) were extracted and purified. Characterization of the purified enzyme showed 2 isoenzymes. One isoenzyme was heat labile, was homoarginine inhibited and had the electrophoretic migration of alkaline phosphatase of human osseous origin. Immunodiffusion showed that this isoenzyme reacted positively only against antibone alkaline phosphatase antibodies. The 2nd isoenzyme was heat stable, was inhibited by phenylalanine and had the same electrophoretic migration as alkaline phosphatase extracted from mature normal human placenta. This 2nd isoenzyme had the same antigenicity as the normal placental enzyme. Like the D-variant placental phenotype, this 2nd isoenzyme was inhibited by L-leucine and EDTA.

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