[Comparative study on activity of adenylate cyclase in normal human ovary with ovarian tumors].
It has been documented that the binding activity sites of human chorionic gonadotropin (HCG) receptor and kd in human ovarian tumors are different from those in the normal ovary. And some observations suggest that the HCG receptor depends on adenylate cyclase (AC) for its physiological functions. We studied the activity of AC in normal human ovary and ovarian tumors. Five human ovarian specimens and eighteen ovarian tumor specimens were obtained from women patients undergoing gynecological surgery. Ovaries were homogenized and sonicated. The homogenates were centrifuged at 1000 x g for 15 min. After sucrose density gradient ultracentrifugation (78000 x g, 4 h), the membrane fraction was collected from interface between 33% and 37%. The membrane protein approximately 10 micrograms, ATP 1 mmol/L, 3H-ATP 5 x 10(4) cpm, sulphydryl-ethyl alcohol 10 mmol/L, in a final volume of 200 microliters of Tris-HCl buffer (50 mmol/L), pH7.5, containing MgSO4 5 mmol/L, were incubated at 35 degrees C for 10 min. The reaction was stopped by boiling water bath for 3 min. The AC activity (U/mg): of human normal ovary, 67 +/- 8, of cystadenocarcinoma serous, 146 +/- 70; of cystadenocarcinoma mucinous, 289 +/- 83.
Qiu
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Chen
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Du
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D000262:Adenylyl Cyclases / Q000378:metabolism*; D003536:Cystadenocarcinoma / Q000201:enzymology*; D005260:Female; D006801:Humans; D008565:Membrane Proteins / Q000378:metabolism; D010051:Ovarian Neoplasms / Q000201:enzymology*; D010053:Ovary / Q000201:enzymology*
D008565:Membrane Proteins; D000262:Adenylyl Cyclases