Title of article :
Glycosidases in the Peritoneal Fluid from Infertile Women With and Without Endometriosis
Author/Authors :
Adriano Brandelli، نويسنده , , EduardoP Passos، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 1998
Pages :
6
From page :
181
To page :
186
Abstract :
Objectives: To investigate the activity and biochemical properties of glycosidases in the peritoneal fluid of infertile patients with or without endometriosis in comparison with fertile women. Design and methods: Peritoneal fluid was collected from 29 women undergoing a laparoscopy. The sample was separated into the following groups: fertile women (n = 11), infertile with endometriosis (n = 11), and infertile without endometriosis (n = 7). The activity of glycosidases was determined with specific p-nitrophenyl-glycosides as colorimetric substrates. Results: The activity of α-fucosidase, α-glucosidase, α-mannosidase, β-galactosidase, β-glucuronidase, and β-N-acetylhexosaminidase was investigated. Enzymatic activities of α-fucosidase and β-N-acetylglucosaminidase were detected in higher amounts than other glycosidases. The activities of α-fucosidase and N-acetylglucosaminidase were increased in the case of infertile patients without endometriosis, while β-galactosidase was increased in endometriosis patients. Enzyme properties as pH optimum, pH stability, thermal stability and inhibition by specific carbohydrates were similar for both control and infertile samples. Analysis of kinetic parameters indicate that Vmax values of glycosidases were higher for infertile samples than their respective controls. Conclusions: The results indicate that higher amounts of glycosidases are present in the peritoneal fluid from infertile patients. The elevated activity of these hydrolytic enzymes suggest possible deleterious effect on gametes, and could explain some cases of infertility.
Keywords :
Infertility , endometriosis , o:-fucosidase , l3-galactosidase , hexosaminidase
Journal title :
Clinical Biochemistry
Serial Year :
1998
Journal title :
Clinical Biochemistry
Record number :
481900
Link To Document :
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