Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

We correlated the activity of alpha-glucosidase in seminal plasma with the motility and differential motility of sperm. Significant positive correlations were found between the alpha-glucosidase activity and both motility and the percentage sperm with good forward progression. This supports the use of alpha-glucosidase in semen as a marker of epididymal function and specifically of the development of motility.
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PMID:Alpha-glucosidase activity and sperm motility. 224 Jun 18

Biochemical analysis was made of specific accessory gland products in the ejaculates of 362 men suffering from various acute inflammatory diseases of the reproductive tract and 33 normozoospermic patients acting as controls. The ejaculate content of the epididymal markers alpha-glucosidase and L-carnitine, but not glycerophosphocholine, was significantly reduced in ejaculates from men with epididymitis; citric acid was reduced in men suffering from prostatitis; both citric acid and alpha-glucosidase were reduced in men suffering from adnexitis. The ejaculate content of epididymal and prostatic markers in prostato-urethritis (adnexitis), where the exact localization of the inflammation was unclear, was not as low as in epididymitis or prostatitis. Seminal vesicle function, as judged from semen volumes and seminal fructose, was not different in these groups of patients. The results, although strongly related to the clinical diagnosis, were unrelated to the microbiological flora of the semen and indicate that both the epididymis and the prostate glands are involved in some forms of adnexitis.
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PMID:The influence of inflammation of the human male genital tract on secretion of the seminal markers alpha-glucosidase, glycerophosphocholine, carnitine, fructose and citric acid. 228 78

We have been able to collect ejaculates from four pre-pubertal Finnish Landrace and Suffolk lambs. Respective seminal plasma alpha-glucosidase specific activity was low (less than 0.3 mU/mg) whatever the season of observation. At puberty, it reached a level higher than 1 mU/mg as observed in adult rams. Administration of alpha-chlorohydrin to 14 adult rams (25 mg/kg/day during 25 days) led to the appearance of immature sperm. Seminal plasma alpha-glucosidase activity dropped from 1.5 to 0.5 mU/mg in both breeds, while fructose was raised from 2 to 6 mg/ml. L-carnitine and blood plasma testosterone remained unchanged during treatment. Semen characteristics appeared normal one month after the end of treatment when fructose concentration decreased simultaneously and enzymatic activity increased during two months to normal levels. The present findings suggest that seminal plasma alpha-glucosidase may be considered as a useful epididymal marker in ram.
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PMID:Effect of physiological (in lamb) or drug-induced (in adult) immaturity of ram spermatozoa on seminal plasma alpha-glucosidase activity. 286 91

L-carnitine, alpha,1-4-glucosidase, and glycerylphosphorylcholine were measured in seminal plasma of a selected group of azoospermic men and in an unselected group of oligozoospermic men. In vasectomized subjects the epididymal indices (mean +/- standard error: L-carnitine, 276.9 +/- 27.5 nmol/ejaculate; alpha-glucosidase, 1.2 +/- 0.1 U/ejaculate; and glycerylphosphorylcholine, 1.5 +/- 0.2 mumol/ejaculate) were always below the normal range of fertile subjects (1757.4 +/- 76.7 nmol/ejaculate; 16.4 +/- 0.9 U/ejaculate; and 17.3 +/- 0.7 mumol/ejaculate, respectively). On the contrary in a large number of patients affected by azoospermia because of seminiferous tubular damage (750.4 +/- 83.6 nmol/ejaculate; 6.8 +/- 0.9 U/ejaculate; and 6.1 +/- 0.6 mumol/ejaculate; respectively) and in a few oligozoospermic subjects (1193.7 +/- 72.3 nmol/ejaculate; 10.3 +/- 0.7 U/ejaculate; and 10.8 +/- 0.7 mumol/ejaculate; respectively) the epididymal indices were found in the range of vasectomized subjects, showing an association between seminiferous tubular lesion and epididymal dysfunction. In conclusion, in spite of the low levels of epididymal indices found in patients with obstructive azoospermia, the presence of a large number of subjects with seminiferous tubular lesions without obstruction with similar low values of L-carnitine, alpha-glucosidase, and glycerylphosphorylcholine reduces the usefulness of these indices in differential diagnosis of azoospermia.
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PMID:Simultaneous measurement of seminal L-carnitine, alpha,1-4-glucosidase, and glycerylphosphorylcholine in azoospermic and oligozoospermic patients. 310 88

5-Br-4-Cl-3-Indoxyl-alpha-D-gluco(pyrano)side was found to be the most suitable synthetic substrate for the demonstration of alpha-D-glucosidases in situ. Using an azoindoxyl procedure with hexazotized pararosaniline or new fuchsine at pH 5 in freeze-dried celloidine-mounted cryostat sections acid alpha-D-glucosidase (EC 3.2.1.20) was shown for the first time in lysosomes of many cells of fetal and adult rat, mouse, guinea-pig, marmoset and human organs. At pH 6.5, in chloroform-acetone pretreated cryostat sections plasma membrane alpha-D-glucosidases were shown in the brush border of enterocytes of the small and large intestine, in the brush border of proximal renal tubule cells and in the stereocilia of the epididymal duct. In an indigogenic procedure with ferricyanide/ferrocyanide as redox catalysator plasma membrane alpha-D-glucosidases were depicted as well as with the azo-indoxyl method; the demonstration of the acid alpha-D-glucosidase was inferior to that achieved with the azo-indoxyl procedure. Using tetrazolium salts as capture reagent intracellular localization was unsatisfactory. In enterocytes, a localization in the Golgi apparatus was shown by the azo-indoxyl procedure only. Analytical isoelectric focusing revealed organ-dependent differences of plasma membrane and lysosomal alpha-D-glucosidases. Compared with the already existing methods the azo-indoxyl and indigogenic procedures are by far the most suitable techniques.
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PMID:Histochemical detection of alpha-D-glucosidases and their molecular forms with 5-Br-4-Cl-3-indoxyl-alpha-D-glucoside. 310 70

1. Ram seminal plasma alpha-glucosidase has been purified in order to increase our knowledge of this enzyme and of its role in epididymal physiology. 2. Since the enzyme behaved differently from other known acid alpha-glucosidases and was not affinity-adsorbed on dextran gels, another approach had to be used. 3. The final procedure included an ethanol precipitation step, sequential chromatography on hydroxylapatite and DEAE Sepharose CL-6B, isoelectric focusing in polyacrylamide gels and ultrafiltration. 4. The resulting purification factor of alpha-glucosidase was 9822 with an overall yield of 5%. 5. The purified material consisted of several isoforms with a mol. wt of 105,000 and isoelectric points varying between 4 and 5.
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PMID:Purification of ram seminal plasma acid alpha-glucosidase. 312 30

Acid alpha-glucosidase and L-carnitine (a well-known epididymal marker) were measured in rete testis and epididymal fluids of adult male rams. These fluids were collected by selective catheterization or by a micropuncture technique, respectively. Both parameters remained at a low and constant level in rete testis and all along caput and corpus epididymidis. Then they increased at equivalent rates in cauda epididymidis to much higher levels than those in seminal plasma (5 mU/mg protein and 10 mM, respectively). An optimum pH study of alpha-glucosidase activity in these fluids showed two well-separated peaks in rete testis and caput epididymal fluids around pH 4 and 7, respectively, but only a single peak at pH 4 in cauda epididymidis that was comparable to the one in seminal plasma. Sucrose density gradient fractions analyzed for their enzyme content in the absence or presence of sodium dodecyl sulfate (1% w/v), a selective inhibitor of acid alpha-glucosidase activity, allowed the demonstration of two enzyme forms at pH 6.8 in rete testis fluid sedimenting in the 7S and 4S regions of the gradient, while a unique 4S form was encountered in cauda epididymidis and in seminal plasma. Although the fate of the minor 7S component of the rete testis fluid in its epididymal transit is presently unknown, similarities between the enzyme in cauda epididymidis and seminal plasma are strong enough to support the hypothesis that epididymis contributes primarily to the acid alpha-glucosidase content of ram seminal plasma.
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PMID:Major contribution of epididymis to alpha-glucosidase content of ram seminal plasma. 389

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

We have studied some characteristics of alpha-1,4-glucosidases in human male reproductive organs in order to obtain information on the origin of the enzyme in seminal plasma. Acid and neutral enzymes could be distinguished on the basis of their selective inhibition either by SDS (acid enzyme) or MTT (neutral enzyme). Only the epididymis contained a significant amount of SDS resistant neutral alpha-1,4-glucosidase which was comparable to what has been isolated in seminal plasma. The similarity of epididymal and seminal plasma neutral enzymes was further confirmed by ultracentrifugation on sucrose density gradients, which permitted a complete separation of neutral (11S) and acid (4S) iso-enzymes. The 11S form was present in epididymis and in seminal plasma, but was totally absent in seminal vesicles, prostates and testis. The epididymal enzyme also had some of the unique characteristics found in the seminal plasma enzyme: it precipitated upon dialysis against distilled water, and its mobility on SDS polyacrylamide gel electrophoresis was identical to that of form 1 in seminal plasma. These results, although they do not constitute absolute proof of the identity of epididymal and seminal plasma alpha-glucosidase, certainly provide strong support for this hypothesis.
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PMID:Similar biochemical properties of human seminal plasma and epididymal alpha-1,4-glucosidase. 638 46

Neutral alpha-1,4-glucosidase catalyzes the breakdown of oligosaccharides in several tissues including the reproductive organs, and we have demonstrated the presence of two molecular forms (F1 and F2) of the enzyme in human seminal plasma. The identification of these forms can be achieved by sucrose density gradient analysis and/or electrophoresis in the presence of detergents. Individuals with normal sperm analyses or affected by a varicocele, thus showing normo- or oligoasthenozoospermia, show a similar prevalence of F1 only and F1 + F2 forms, while the presence of F2 alone becomes obvious following vasectomy. In conclusion, molecular forms of the enzyme do not appear to be indicative of the presence of a varicocele, but they may reflect modifications in the secretory function of specific reproductive organs (prostate) or glands (seminal vesicles), as observed in the course of an obstructive abnormality at the epididymal or vas deferens level.
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PMID:Neutral alpha-1,4-glucosidase in human seminal plasma: molecular forms in varicocele and after vasectomy. 674 56


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