N-Acetyl-beta-glucosaminidase activity in hydatidiform mole. |
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Authors: | K C Leung K P Fung C C Yu Y M Choy C Y Lee |
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Affiliation: | Departments of Clinical Chemistry and Medicine, Lasarettet, S-251 87 HelsingborgSweden |
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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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Keywords: | S-ASAT S-aspartate aminotransferase S-LD S-lactate dehydrogenase S-CK S-creatine kinase |
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