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:3.1.3.5 (5'-nucleotidase)
3,167 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Patients with jaundice and hyperbilirubinemia over 34 mumol/l have been examined by different methods in order to assess the diagnostic value of the methods. 340 patients were examined clinically and by laparoscopy, 168 patients and 92 healthy persons were examined by 10 laboratory indices, 639 patients--by ultrasonography, 95 patients--by scintigraphy, 116 patients--by computer tomography, 83 patients--by endoscopic retrograde cholangio-pancreatography (ERCPG), 17 patients--by percutaneous transhepatic cholangiography (PTC), 70 patients--by directed liver biopsy. In the patients with cholestasis the 5'-nucleotidase, alkaline phosphatase, glutamyl transpeptidase (lipoprotein X is positive in 92% of the patients) and cholesterol are increased most. The extrahepatic obstructions are diagnosed by ultrasonography in 94.8% of the patients (the biliary ducts are dilated), in 88.7% of the patients the localization of the obstruction and in 74.7% of the patients the cause of the obstruction are found. In parenchymal jaundice the sonography reveals the disease which has caused jaundice in 62.1% of the patients. The scintigraphy gives correct diagnosis in 50% of the patients with hepatitis and jaundice, in 78% of the patients with cirrhosis and jaundice and in 87.5% of the patients with liver cancer. The computer tomography reveals the obstructive jaundice in 94.7% of the patients and the focal processes in the liver in 96.7% of the patients. The ERCPG gives a clear picture of the biliary ducts in 72.28% and of the pancreatic duct in 83.13% of the patients with jaundice, simultaneously the biliary and the pancreatic ducts--in 45.78% of the patients and correct diagnosis in 83.1% of the patients examined.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[Differential diagnosis of jaundice]. 343 27

1. At 30 weeks of age, homozygote diabetic C57 BL KsJ (db/db) mice were grossly obese, lethargic and displayed moderate hair loss relative to heterozygote control C 57 BL KsJ (db/+) mice. 2. In diabetic mice, compared to control, the total body weights, liver weight: body weight ratios, and blood glucose levels were increased 2.3 fold, 20% and 3.1 fold, respectively. 3. Analysis of plasma membranes isolated from control and diabetic mouse liver established that comparable purity levels were achieved since relative specific activities of the plasma membrane markers 5'-nucleotidase and gamma-glutamyltranspeptidase were similar: 10.2 and 11.4 fold with respect to 5'-nucleotidase in control and diabetic states respectively; and 8.0 and 8.3 fold with respect to gamma-glutamyltranspeptidase in control and diabetic states respectively. 4. A select effect of diabetes on gamma-glutamyltranspepetidase, however, was observed. The activity of this enzyme was found to be reduced 16% in diabetic liver compared to control liver. 5. Assessment of [3H]prazosin and [3H]dihydrolalprenolol binding to mouse liver plasma membranes indicated that although there was no difference in beta-adrenergic receptor binding in control and diabetic states, alpha 1-adrenergic receptor binding was found to be reduced 43% in diabetic mouse liver plasma membranes. 6. Scatchard analyses of kinetic studies indicate that the reduction is a reflection of decreases in alpha 1-adrenergic receptor numbers with no change in alpha 1 receptor affinity in the diabetic state: since for diabetic and control liver plasma membranes, Kd values were 3.41 +/- 0.02 nM and 3.40 +/- 0.01 nM respectively; and Bmax were 650.12 +/- 16.44 fmol mg-1 and 380.76 +/- 12.92 fmol mg-1, respectively.
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PMID:Hepatic adrenergic receptors in the genetically diabetic C57 BL/KsJ (db/db) mouse. 343 80

Biopsy specimens from all main segments of the large bowel, obtained from 16 patients with ulcerative colitis, were examined histologically and assayed for a series of organelle marker enzymes. Compared with a control group of 20 subjects, significant dependence on diagnosis was demonstrated for N-acetyl-beta-D-glucosaminidase (p less than 0.01) and monoamine oxidase (p less than 0.05), when dependence on segment was taken into account. Significant correlation with degree of inflammatory cell infiltration was seen in the gamma-glutamyltransferase (p less than 0.0001), 5'-nucleotidase (p less than 0.05), and monoamine oxidase (p less than 0.0001) activities. Patients with dysplasia had lower activity of N-acetyl-beta-D-glucosaminidase (p less than 0.05) than those without dysplasia when evaluated by two-way analysis of variance modified for repeated measurements. Multienzyme analysis could distinguish between specimens with dysplasia and aneuploidy and those without when discriminant analyses were used.
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PMID:Enzyme activities in biopsy specimens from large-bowel mucosa in ulcerative colitis. 360 24

Biopsy specimens from 29 adenomas, 17 adenocarcinomas, and 6 synchronous adenomas in cancer patients and from uninvolved mucosa of all main segments of the large bowel were examined histologically and assayed for a series of organelle marker enzymes. Six enzymes--lactase, sucrase, alkaline phosphatase, 5'-nucleotidase, acid phosphatase, and N-acetyl-beta-D-glucosaminidase--showed less activity in adenomas than in adjacent uninvolved mucosa and in specimens from controls. Cancer tissue had higher gamma-glutamyltransferase and lower lactase, alkaline and acid phosphatases, and N-acetyl-beta-D-glucosaminidase activities than specimens from uninvolved mucosa in cancer patients and control patients. Enhanced alkaline phosphatase and N-acetyl-beta-D-glucosaminidase activities were seen in uninvolved mucosa of cancer patients as compared with those of adenoma and control patients. Evidence has been found for multienzyme analysis to identify adenomas with signs of malignant transformation and carcinomas with poor prognosis.
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PMID:Enzyme activities in biopsy specimens from large-bowel mucosa in colorectal adenomas and carcinomas. 362 77

Using microvillous membrane vesicles prepared from human normal early and full term placenta, we investigated the transport mechanism of L-alanine and the change in its transport activity during gestation. We estimated the purity of microvillous membrane vesicles prepared from human placenta from the relative specific activities (microvilli versus homogenate) of the membrane's maker enzymes, alkaline phosphatase (ALP), 5'-nucleotidase, and gamma-glutamyltranspeptidase ( gamma-GTP). In early pregnancy (12-15 weeks gestational age), the relative specific activities (microvilli versus homogenate) were calculated to be: ALP: 15.3, 5'-nucleotidase: 14.0, gamma-GTP: 8.3, and in full term pregnancy (37-40 weeks gestational age) the relative specific activities (microvilli versus homogenate) were calculated to be: ALP: 16.0, 5'-nucleotidase: 14.8, gamma-GTP: 7.5. The uptake of L-alanine into microvillous membrane vesicles was Na+ electrochemical gradient (extravesicular greater than intravesicular) dependent and this Na+ dependent uptake was membrane-potentially sensitive both in early pregnancy and in full term pregnancy. The kinetics parameter of the initial L-alanine uptake into microvillous membrane vesicles were calculated to be: Km: 0.78 +/- 0.20 mM, Vmax: 0.62 +/- 0.21 nmol/mg protein/20 sec in early pregnancy, Km: 0.80 +/- 0.24 mM, Vmax: 3.53 +/- 0.70 nmol/mg protein/20 sec in full term pregnancy. In conclusion, the placental transport mechanisms of L-alanine in both early and full term pregnancy were the same, and the L-alanine transport activity of full term pregnancy was much greater than that of early pregnancy.
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PMID:[Study on changes in placental L-alanine transport activity during gestation (using microvillous membrane vesicles]. 370 Nov 43

The distribution of a series of mucosal enzymes along the large bowel was studied by analysis of homogenized biopsy specimens from five different segments, obtained from 20 control patients. The activities varied significantly between the segments for the membrane enzymes lactase (p less than 0.005), alkaline phosphatase (p less than 0.0005), leucyl-beta-naphthylamidase (p less than 0.0001), and 5'-nucleotidase (p less than 0.001) and the mitochondrial enzyme monoamine oxidase (p less than 0.0005) when tested by analysis of variance modified for repeated measurements. When paired comparisons between segments were evaluated, the enzyme activities of the proximal large bowel were significantly higher than those of distal segments. The levels of sucrase, neutral-alpha-glucosidase, gamma-glutamyltransferase, and lysosomal enzymes remained unchanged throughout the large intestine, as did the protein to DNA ratio. The results are compatible with the theory that different segments of the large bowel have different functions.
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PMID:Longitudinal distribution of mucosal enzymes in the human large bowel. 377 57

Biopsy specimens from the antral and body part of the stomach were studied for a range of marker enzymes in 11 patients with superficial gastritis, 9 patients with atrophic gastritis, and 31 Billroth-II-resected patients and compared with activities found in controls with normal gastric mucosa. In the antral part of the stomach increased gamma-glutamyltransferase activity was found in superficial (p less than 0.01) and atrophic gastritis (p less than 0.05), whereas monoamine oxidase activity was decreased in superficial (p less than 0.01) and atrophic gastritis (p less than 0.05). In the body part, increased activity of gamma-glutamyltransferase (p less than 0.01) and acid-beta-glucuronidase (p less than 0.01) was found in superficial gastritis. In atrophic gastritis increased activities for lactase (p less than 0.01), alkaline phosphatase (p less than 0.05), leucyl-beta-naphthylamidase (p less than 0.05), gamma-glutamyltransferase (p less than 0.05), 5'-nucleotidase (p less than 0.01), N-acetyl-beta-D-glucosaminidase (p less than 0.05), and acid-beta-glucuronidase (p less than 0.01) were found. Specimens from the gastric remnant showed an enzyme activity pattern similar to that seen in the body in atrophic gastritis, apart from a significantly decreased monoamine oxidase activity (p less than 0.004). Specimens with dysplasia in the gastric remnant showed decreased monoamine oxidase activity when compared with specimens without dysplasia (p less than 0.01).
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PMID:Enzyme activities in human gastric mucosa in gastritis and resected stomachs. 381

The distribution of a series of marker enzymes in the gastric mucosa was studied by analysis of homogenized biopsy specimens from the lesser and greater curvature of the body and antrum, respectively, obtained from 11 control patients. The activities varied significantly between the regions for the membrane enzymes lactase (p less than 0.0001), neutral-alpha-glucosidase (p less than 0.005), alkaline phosphatase (p less than 0.01), leucyl-beta-naphthylamidase (p less than 0.005), and 5'-nucleotidase (p less than 0.0001) and the lysosomal enzymes N-acetyl-beta-D-glucosaminidase (p less than 0.0001) and acid beta-glucuronidase (p less than 0.0001), using analysis of variance modified for repeated measurements. When paired comparisons between regions were evaluated, the enzyme activities of the antral regions were significantly higher than those of the body stomach. The activities of gamma-glutamyltransferase, acid phosphatase, and the mitochondrial enzyme monoamine oxidase did not alter between regions, nor did the protein to DNA ratio. The demonstrated biochemical distinction between antrum and body of the stomach may be explained by different physiological and histological properties of the two parts.
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PMID:Enzyme activities in biopsy specimens from human gastric mucosa. 381 4

Purified plasma membranes of mouse EL4 lymphoma cells were fractionated by means of affinity chromatography on concanavalin A-Sepharose into two subfractions; one (MF1) eluted freely from the affinity column, the second (MF2) adhered specifically to Con A-Sepharose. Both membrane subfractions proved to be of plasma membrane origin, as evidenced by the following criteria. (i) The ratio of cholesterol to phospholipid was nearly identical in plasma membrane and both subfractions. (ii) When isolated plasma membranes were labelled with tritiated NaBH4, both subfractions exhibited identical specific radioactivities. (iii) After enzymatic radioiodination of the cells, the total content of labelled proteins was very similar in isolated plasma membranes and in both subfractions. (iv) Some plasma membrane marker enzymes exhibited nearly identical specific activities in plasma membranes, MF1 or MF2 including gamma-glutamyl transpeptidase, 5'-nucleotidase and Mg2+-ATPase. Both subfractions exhibited characteristic differences. Thus the specific activities of (Na+ + K+)-ATPase, Ca2+-ATPase and lysophosphatidylcholine acyltransferase were several-fold enriched in MF2 compared to MF1. SDS-polyacrylamide gel electrophoresis revealed a different polypeptide composition of the two subfractions. Polypeptides of apparent molecular mass of 116, 95, 42, 39, 30 and 28 kDa were highly enriched in MF2, whereas MF1 contained another set of proteins, of apparent molecular mass of 70, 55 and 24 kDa. The phospholipid fatty acid composition of the subfractions proved to be different, as well, MF2 contained more saturated fatty acids than MF1. The data suggest the existence of plasma membrane domains in the plasma membranes of the mouse EL4 lymphoma cells, containing a set of polypeptides, among others membrane bound enzymes, embedded in a different phospholipid milieu.
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PMID:Characterization of plasma membrane domains of mouse EL4 lymphoma cells obtained by affinity chromatography on concanavalin A-Sepharose. 407 40

1. A method for the preparation of brush border from rabbit kidneys is described. Contamination by other organelles was checked by electron microscopy and by the assay of marker enzymes and was low. 2. Seven enzymes, all hydrolases, were substantially enriched in the brush-border preparation and are considered to be primarily located in this structure. They are: alkaline phosphatase, maltase, trehalase, aminopeptidase A, aminopeptidase M, gamma-glutamyl transpeptidase and a neutral peptidase assayed by its ability to hydrolyse [(125)I]iodoinsulin B chain. 3. Adenosine triphosphatases were also present in the preparation, but showed lower enrichments. 4. Alkaline phosphatase was the most active phosphatase present in the preparation. The weak hydrolysis of AMP may well have been due to this enzyme rather than a specific 5'-nucleotidase. 5. The two disaccharidases in brush border were distinguished by the relative heat-stability of trehalase compared with that of maltase. 6. The individuality of the four peptidases was established by several means. The neutral peptidase and aminopeptidase M, both of which can attack insulin B chain, differed not only in response to inhibitors and activators but also in the inhibitory effect of a guinea-pig antiserum raised to rabbit aminopeptidase M. This antiserum inhibited both the purified and the brush-border activities of aminopeptidase M. The neutral peptidase and gamma-glutamyl transpeptidase were unaffected but aminopeptidase A was weakly inhibited. The characteristic responses to Ca(2+) and serine with borate served to distinguish aminopeptidase A and gamma-glutamyl transpeptidase from other peptidases. 7. No dipeptidases, tripeptidases or carboxypeptidases were identified as brush-border enzymes. 8. Incubation of brush border with papain released almost all the aminopeptidase M activity but only about half the activities of maltase, gamma-glutamyl transpeptidase and aminopeptidase A. No release of alkaline phosphatase, trehalase or the neutral peptidase was observed.
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PMID:Studies on the enzymology of purified preparations of brush border from rabbit kidney. 414 72


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