Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.20 (alpha-glucosidase)
4,237 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A synthetic substrate (p-nitrophenyl-alpha-D-glucopyranoside) was used to measure the acid and neutral alpha-glucosidase activity in bull seminal plasma, spermatozoa and in homogenates of bull reproductive organs. Marked differences were observed in the activities of these enzymes in the various tissues studied. Epididymis and particularly its caput region contained the highest specific activity of acid alpha-glucosidase. The activity of neutral alpha-glucosidase was highest in testis and in different parts of the epididymis. Seminal plasma, spermatozoa and seminal vesicle secretion contained only the acid enzyme activity. After fractionation with anion exchange chromatography in HPLC (Mono Q) and chromatofocussing, acid alpha-glucosidase activity of seminal plasma was recovered in two fractions with different pI values. The corresponding activities were found in the secretion of seminal vesicles, which thus form the major secretory source of seminal plasma acid alpha-glucosidase. In the fractionation with gel filtration on Sepharose 6B, the acid alpha-glucosidase had a smaller molecular weight than did the neutral enzyme. In anion exchange chromatography and chromatofocussing the testicular and epididymal homogenates each contained two acid and two neutral isoenzymes. In both fractionations the elution pattern of acid alpha-glucosidase was clearly different from that of the enzymes in seminal plasma. The pH optimum of acid alpha-glucosidase ranged from 3.75 to 4.5 and that of the neutral enzyme from 6.5 to 7.0. The neutral activity was more sensitive to many divalent metal ions and differences were also observed in the response of the enzymes to different concentrations of turanose and KCl.
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PMID:Acid and neutral alpha-glucosidase in the reproductive organs and seminal plasma of the bull. 390 Mar 85

Di-n-butyl phthalate (DBP) is a ubiquitous environmental pollutant, extensively used as a plasticizer in many products including plastics, cosmetics and medical devices. Previous studies have shown that DBP has potential testicular toxicity. Epididymis is known to play an important role in the maturation and storage of sperm. However, the effect and mechanism of action of DBP on epididymis is unclear. The present study was designed to investigate the effect of DBP on structure and function of epididymis in adult male rats by histological and biochemical study. Oxidative stress was also assessed in rat epididymis as an underlying mechanism. Forty SD adult rats were randomly allotted to four groups, and DBP was administered to each group by oral gavage at doses of 0 (control), 100, 250 and 500 mg/kg/day for 2 consecutive weeks. The results indicated that the epididymal toxicity of DBP is dose-dependent. Epididymal weight, activities of epididymal alpha-glucosidase and glutathione peroxidase (GSH-Px) was significantly decreased in rats of 500 mg/kg DBP exposure group compared to the control. The activity of superoxide dismutase (SOD) was significantly decreased while the level of malondialdehyde (MDA) was significantly increased in the epididymal tissue of the 250 and 500 mg/kg DBP exposure groups compared with the control group. Moreover, microscopy with hematoxylin and eosin (HE) staining showed that atrophy of epididymal tubules, the interstitial vascular was hyperemia and the lumina were oligozoospermic in rats of 500 mg/kg DBP exposure group. In conclusion, DBP exposure alters the epididymal structure and function by inducing oxidative stress in epididymis of adult rats.
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PMID:Di-n-butyl phthalate (DBP) exposure induces oxidative stress in epididymis of adult rats. 2082 52