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)

The activities of various glycosidases in homogenates of the small intestinal mucosa of two adult and 18 suckling tammar wallabies (M. eugenii) aged from 6 to 50 weeks were investigated. Lactase (beta-D-galactosidase), beta-N-acetylglucosaminidase, alpha-L-fucosidase and neuraminidase activities were high during the first 34 weeks post partum and then declined to very low levels. Maltase, isomaltase, sucrase and trehalase activities were very low or absent during the first 34 weeks, and then increased. The lactase activity was unusual in being greater in the distal than the middle or proximal thirds of the intestine, and in its low pH optimum (pH 4.6), inhibition by p-chloromercuribenzene sulfonate but not by Tris, and lack of cellobiase activity. These properties are those of a lysosomal acid beta-galactosidase rather than of a brush border neutral lactase. The maltase activity had the characteristics of a lysosomal acid alpha-glucosidase early in lactation and of a brush border neutral maltase in adult animals. The significance of these findings is discussed in relation to changes in dietary carbohydrates during weaning and to the mode of digestion of milk carbohydrates by the pouch young.
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PMID:Intestinal lactase (beta-galactosidase) and other glycosidase activities in suckling and adult tammar wallabies (Macropus eugenii). 678 21

The specific activities of several glycosidases (beta-N-acetylglucosaminidase, beta-D-glucosidase, alpha-D-glucosidase, beta-D-fucosidase, alpha-L-fucosidase and beta-D-galactosidase) were determined in human sera from a control group to 10 normal subjects and in four groups, each of 10 patients, with acute viral hepatitis, acute pancreatitis, acute myocardial infarction and breast cancer. The results show significantly higher activities in acute viral hepatitis for beta-N-acetylglucosaminidase, beta-D-glucosidase and alpha-D-glucosidase (p less than 0.001); in acute pancreatitis for the first two of these enzymes (p less than 0.001); and in breast cancer for beta-D-glucosidase (p less than 0.001). Further, lower differences were found in the patients with acute viral hepatitis for beta-D-fucosidase and alpha-L-fucosidase (p less than 0.01); in acute myocardial infarction for beta-N-acetylglucosaminidase, beta-D-glucosidase, alpha-D-glucosidase, beta-D-fucosidase and beta-D-galactosidase (p less than 0.01, p less than 0.05, p less than 0.05, p less than 0.01 and p less than 0.01, respectively); and in breast cancer for beta-N-acetylglucosaminidase (p less than 0.01). No significant differences were found for the other glycosidases.
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PMID:Serum beta-N-acetylglucosaminidase, beta-D-glucosidase, alpha-D-glucosidase, beta-D-fucosidase, alpha-L-fucosidase and beta-D-galactosidase levels in acute viral hepatitis, pancreatitis, myocardial infarction and breast cancer. 680 Jun 74

The activities of seven lysosomal enzymes (alpha-D-glucosidase, beta-D-galactosidase, beta-D-glucuronidase, hexosaminidase, alpha-L-fucosidase, alpha-D-mannosidase, acid phosphatases) were studied in the serum of 31 untreated patients with Graves' disease, 30 treated hyperthyroid patients whose clinical abnormalities had disappeared and whose hormones had returned to euthyroid levels, and 34 controls. The hyperthyroid state is characterized by increased serum levels of alpha-D-glucosidase, beta-D-glucuronidase, hexosaminidase and especially of alpha-L-glucosidase and alpha-D-mannosidase. In contrast, neither beta-D-galactosidase nor acid phosphatases serum levels were significantly modified. After antithyroid treatment, the activities of these enzymes returned to normal levels, except for alpha-D-mannosidase. The interpretation of these changes in serum acid hydrolases activities is controversial.
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PMID:Serum lysosomal acid hydrolase activities in Graves' disease. 680 24

Nine lysosomal enzymes and alkaline phosphatase have been assayed in human pancreatic juice from controls and patients with chronic calcifying pancreatitis. Specific activities were evaluated by a nonparametric test (Wilcoxon) with a probability of 2 P less than or equal to 0.5. The values of acid phosphatase, alpha-glucosidase, beta-glucosidase and alpha-galactosidase are significantly higher in pathological juices; the values of alpha-mannosidase and beta-glucuronidase are also increased in the same patients but at the limit of significance. Alkaline phosphatase, beta-hexosaminidase and alpha-fucosidase follows the same trend but the values are not statistically significant between the two groups of patients. Studies on skin cultures of four patients with chronic calcifying pancreatitis demonstrate that the increased specific activities of lysosomal enzymes in the pathological juices do not correspond to a leakage of these enzymes into the extracellular space as described for cystic fibrosis.
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PMID:Alkaline phosphatase and acid lysosomal hydrolases in pancreatic juice and fibroblast cell cultures of patients with chronic calcifying pancreatitis. 680 85

Spontaneously diabetic non-obese mice of the ICR strain were newly inbred in Shionogi laboratory, Japan. Animals became diabetic suddenly, more frequently and severely in females. Blood glucose levels were 452 +/- 73 mg/100 ml with serum insulin levels of less than 1.0 microU/ml in the fed state. Parabiosis with normal control ICR mice for 2 weeks decreased the blood glucose level to 260 +/- 51 mg/100 ml (P less than 0.01) and resulted in serum insulin levels of 46.0 +/- 18.0 microU/ml (P less than 0.01). Kidney homogenate beta-N-acetylglucosaminidase and beta-galactosidase activities were reduced in diabetic mice (42% and 44% decreases respectively) (P less than 0.025 and P less than 0.001), and restored almost to normal after 2 weeks of parabiosis. Renal alpha-mannosidase activity was decreased 43% (P less than 0.001) in the diabetic mice but unaffected by parabiosis. Serum beta-N-acetylglucosaminidase, beta-galactosidase and alpha-glucosidase activities were significantly increased in diabetic mice (179%; 233% and 58% increase respectively) (P less than 0.005, P less than 0.001 and P less than 0.001), and returned to normal with parabiosis.
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PMID:The effects of parabiosis on serum and kidney glycosidase activities in spontaneously diabetic mice. 699 68

We are studying the biosynthesis and processing of acid hydrolases from Dictyostelium discoideum. We prepared antibody to highly purified alpha-mannosidase from the spent medium of stationary phase cultures. It precipitated alpha-mannosidase but not beta-hexosaminidase, alpha-glucosidase, beta-glucosidase, or any of the major proteins in cell lysates or secretions. The antibody precipitated a 150,000- and an 80,000-dalton protein in addition to mature forms (56,000-62,000 daltons) of alpha-mannosidase subunits. The possibility that the 150,000 and 80,000 dalton bands were precursors of mature forms was evaluated by pulse-chase experiments. Following a 20-min pulse labeling period, only the 150,000-dalton protein was detected in the immunoprecipitate. Apparent conversion of this form into 80,000- and 60,000-dalton forms was observed following a 30-min chase. During the next 90 min continued accumulation of 60,000-dalton and appearance of 62,000-dalton forms was observed while the 80,000-dalton form disappeared. The fate of the 150,000-dalton precursor depended on nutritional conditions. In cells conditioned with fresh growth medium intracellular processing predominated. Less than 10% of either the precursor or mature forms was secreted in 8 hr. However, when cells were shifted from growth medium to starvation buffer, secretion of precursor soon predominated. After a 1-hr lag period, cells began secreting 150,000-dalton precursor into the medium. After 4 hr in starvation buffer, the rate of secretion of 150,000-dalton form increased by at least an order of magnitude while processing was markedly diminished. This may be a case where nutritional conditions control the sorting of an acid hydrolase precursor.
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PMID:Processing and secretion of alpha-mannosidase forms by Dictyostelium discoideum. 705 Jan 3

Biochemical studies of middle ear effusions have demonstrated generally higher levels of certain hydrolytic and oxidative enzymes in mucoid fluids when compared to serous. We have extended these studies by analyzing middle ear effusions for the content of a large number of lysosomal hydrolases. The mean specific activity for alpha-glucosidase in mucoid fluids was found to be ten times that for serous fluids while alpha-mannosidase, beta-glucuronidase, hexosaminidase, acid phosphatase, beta-galactosidase, alkaline phosphatase, and lactate dehydrogenase were found to be three to five times greater in mucoid than serous effusions. In this study the specific enzyme activities for lysosomal hydrolases from purulent effusions were found to be intermediate between the activities in serous and mucoid effusions. No significant correlation was found between the specific activities of lysosomal hydrolases and the presence or absence of bacteria in mucoid or serous middle ear effusions. The hexosaminidase isozyme distribution was found to be identical for serous and mucoid fluids and similar to that found in human serum. However, the isozyme pattern of beta-glucuronidase in mucoid effusions was significantly different than that in normal human serum as mucoid fluids contain a large amount of an anionic isoenzyme of beta-glucuronidase that is barely detectable in human serum.
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PMID:Lysosomal hydrolases in middle ear effusions. 722 13

The activity of particulate neuraminidase (sialidase, EC 3.2.1.18) in wild-type mice and the neurological mutant Staggerer was studied during development. Peak activity of this enzyme was observed at postnatal day 3 (P3) in three tissues of normal mice: cerebellum, cerebrum, and liver. In Staggerer, however, neuraminidase peak activity was observed at P27 in the cerebellum, whereas the activity was close to normal in Staggerer cerebrum and liver. Activities of the other glycosidases in Staggerer (alpha-glucosidase (pH 3.7), alpha-glucosidase (pH 6.0), N-acetyl-beta-hexosaminidase, beta-glucosidase, and beta-galactosidase) did not show significant variation compared with wild-type at P27 in any of the three tissues. This indicates that the late activity peak of particulate neuraminidase activity in the Staggerer cerebellum is neuraminidase-specific and not due to a general increase of lysosomal enzymes.
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PMID:Changes in particulate neuraminidase activity during normal and staggerer mutant mouse development. 726 67

The importance of bacterial vaginosis as a risk factor in obstetric and gynecological infections has recently been recognized. The bacterial vaginosis group of organisms includes members of the Streptococcus milleri group, the identification of which has caused much confusion. We prospectively surveyed the rates of carriage of S. milleri group organisms in 397 high vaginal swabs received in our laboratory. For the identification of 99 clinical isolates and 23 control strains, we compared the results obtained by the rapid ID 32 Strep system (Analytab Products) and by a scheme utilizing six differential phenotypic characteristics (presence of beta-N-acetylglucosaminidase, alpha-glucosidase, beta-D-fucosidase, beta-galactosidase, beta-N-acetylgalactosaminidase, and beta-glucosidase) as described by Whiley et al. (R. A. Whiley, H. Fraser, J. M. Hardie, and D. Beighton, J. Clin. Microbiol. 28:1497-1501, 1990). We identified Streptococcus anginosus in 18% and Streptococcus constellatus in 0.05% of the specimens examined. Of the isolates of S. anginosus that reacted with grouping antisera, 20 of 25 belonged to Lancefield group F. The incubation conditions for bacterial cultures and for reaction mixtures affected the results of phenotypic characterization in the production of alpha-glucosidase, beta-galactosidase, and beta-glucosidase. However, by using bacterial cultures grown under hypercapnic conditions and incubating the reaction mixtures aerobically, consistent phenotypic characteristics were obtained, allowing identification similar to that obtained by the ID 32 Strep system. We therefore recommend the phenotypic scheme as an inexpensive, reliable, and convenient method for the initial identification of species of the S. milleri group.
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PMID:Species identification of members of the Streptococcus milleri group isolated from the vagina by ID 32 Strep system and differential phenotypic characteristics. 765 Jan 93

The way in which the human epididymis modifies spermatozoa during their sojourn in this structure might be clarified by knowledge of the nature of its secretions. We have examined the presence of several lysosomal hydrolases in human epididymal tissue and fluids, and their synthesis and secretion by monolayer cultures. Tissues were obtained from men undergoing orchidectomy for prostatic carcinoma. The enzymes cathepsin D and acid alpha-glucosidase were localised in the lysosomes of epithelial cells from the corpus epididymidis, by an immunocytochemical technique. Cathepsin D was also found in epithelial cells of the efferent ducts within lysosomes, apical vesicles and multivesicular bodies. No immunolocalisation of acid glucosidase in the efferent ducts or on the microvilli of the corpus was demonstrable. Cathepsin D, beta-hexosaminidase (N-acetylglucosaminidase) and alpha-glucosidase were measurable in the luminal fluid from the human corpus epididymidis; beta-hexosaminidase was secreted into the culture medium by confluent monolayers of epididymal and efferent duct cells. Immunoprecipitation of cell extracts and culture medium of these cultures incubated with 35S-methionine revealed that the precursors of cathepsin D and beta-hexosaminidase were synthesized and secreted by such monolayers. Thus, active lytic enzymes are secreted by the human epididymis and could modify sperm membranes.
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PMID:Immunocytochemical localisation of some lysosomal hydrolases, their presence in luminal fluid and their directional secretion by human epididymal cells in culture. 778 Oct 38


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