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    • Keywords


      Human placenta; alkaline phosphatase; 5’-nucleotidase

    • Abstract


      Activities and a few properties of alkaline phosphatase and 5’-nucleotidase were compared in the developing human placenta. Both the enzymes were mostly membrane-bound and displayed similar developmental patterns with the highest activities at 24/26 weeks of the placenta. L-Phenylalanine, L-tryptophan and L-leucine were inhibitors of alkaline phosphatase, whereas they had no effect on the 5’-nucleotidase. Alkaline phosphatase from a late stage of gestation appeared to be almost heat-stable. An appreciable part of 5’-nucleotidase was also resistant to heat inactivation and this fraction varied with gestational age of the tissue. For both the enzymes, Vmax changed without alteringKm values with periods of gestation. Ca2+, Mg2+ and Mn2+ ions stimulated the alkaline phosphatase activity and Hg2+, Zn2+, Cu2+, Ni2+ were inhibitory. 5’-Nucleotidase was not activated by any of these cations. EDTA and Concanavalin A inhibited both the enzymes, although the extent of inhibition was different and also varied with gestation.

    • Author Affiliations


      A S Chakraborti1 P Roychowdhury1 A Das1 M Mukherjea1

      1. Department of Biochemistry, University College of Science, 35, Ballygunge Circular Road, Calcutta - 700 019
    • Dates

  • Journal of Biosciences | News

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      Posted on July 25, 2019

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