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Comparative Study
. 1977 Jan 3;74(1):43-9.
doi: 10.1016/0009-8981(77)90386-2.

N-Acetyl-beta-glucosaminidase activity in hydatidiform mole

Comparative Study

N-Acetyl-beta-glucosaminidase activity in hydatidiform mole

K C Leung et al. Clin Chim Acta. .

Abstract

The N-acetyl-beta-glucosaminidase activity in hydatidiform mole is two-fold higher than that in full-term placenta. Qualitatively, the enzymes from the two tissues are similar with respect to KM values and pH optima. Both enzymes also contain a new isoenzyme form detectable by polyacrylamide gel electrophoresis. However, the molar enzyme is more susceptible to heat denaturation, presumably due to the presence of a higher level of the heat-labile isoenzyme form A in this tissue. Data are also presented incicating that the placenta is not the source of the N-acetyl-beta-glucosaminidase activity in maternal serum.

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