N-Acetyl-beta-glucosaminidase activity in hydatidiform mole.
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.
D000118:Acetylglucosaminidase / Q000378:metabolism*; D004355:Drug Stability; D005260:Female; D006596:Hexosaminidases / Q000378:metabolism*; D006801:Humans; D006828:Hydatidiform Mole / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000378:metabolism; D007700:Kinetics; D010920:Placenta / Q000201:enzymology*; D011247:Pregnancy; D011262:Pregnancy Trimester, Second; D014594:Uterine Neoplasms / Q000201:enzymology*
D007527:Isoenzymes; D006596:Hexosaminidases; D000118:Acetylglucosaminidase