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:3.1.26.9 (ribonuclease)
6,589 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Cystic fibrosis (CF) is a chronic genetic disease mainly affecting the exocrine glands. Its main clinical symptoms are: abnormal production of mucus which blocks the airways, pancreatic insufficiency and increased sweat electrolytes. In the present investigation a series of enzymes and metabolites--mainly of carbohydrate metabolism--was investigated in biological fluids from CF homozygotes, CF heterozygotes and healthy controls under different conditions. CF homozygotes--and to a lesser degree CF heterozygotes--had increased activity of ribonuclease, and increased concentrations of electrolytes and lactate in their saliva and urine at rest. Saliva of CF patients also had augmented levels of protein. When healthy persons were submitted to anaerobic effort, the activity of ribonuclease and the concentrations of protein, electrolytes and lactate increased in their saliva, and thereby, mimicked the values found in the saliva of cystic fibrosis patients at rest. An abnormal response to a sucrose load was found in both CF-homozygotes and CF-heterozygotes. Greater increase in both glucose and lactate concentrations in the blood as well as a more rapid clearance of these metabolites was observed after the sucrose intake. A possible cause for these findings could be a disturbed carbohydrate metabolism in CF. Therefore, enzymes and metabolites connected to the metabolic pathway of glucose were investigated in CF fibroblasts and in animal models for CF. An increased activity of glycolytic enzymes in CF fibroblast were shown. Similar increases in activities of glycolytic enzymes were found in cells of submandibular glands of rats that were killed in a state of induced metabolic acidosis. These cells also showed increased protein and mucus contents, and elemental changes similar to those observed in fibroblasts of cystic fibrosis patients. Contrary to this, decreased activities of the enzymes of the glycolytic pathway were found in the submandibular gland of chronically reserpinized rats. The end-products of glycolysis, pyruvate and lactate, were also decreased, whereas the concentration of phosphoenolopyruvate and creatinphosphate were increased, possibly causing acidosis in the gland. Thus a disturbed glycolytic pathway in CF cells and a decreased intracellular pH might play an important role in the pathogenesis of this disease.
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PMID:Cystic fibrosis. Carbohydrate metabolism in CF and in animal models for CF. 347 61

Some of the enzymes and metabolites of the glycolytic pathway of an animal model for cystic fibrosis (the chronically reserpine-treated rat) were investigated. The activities of the enzymes phosphofructokinase (P less than 0.002), enolase (P less than 0.03), pyruvate kinase (P less than 0.005), and lactate dehydrogenase (P less than 0.009) were decreased whereas the activity of glycerol-3-phosphate dehydrogenase was unaffected in the submandibular glands of the treated animals. For metabolites, the reserpine treatment resulted in an increased concentration of glycogen (P less than 0.0002) and phosphoenolpyruvate (P less than 0.001) and a decreased concentration of pyruvate (P less than 0.005) and lactate (P less than 0.002) in the glands. The concentration of glucose and glycerate-2-phosphate was unaffected. The perchloric acid-soluble part of the proteins was also increased (P less than 0.0001) in the submandibular glands of the reserpine-treated animals, as was the activity of ribonuclease. These findings point to a disturbance in the metabolism of glucose and a possible acidosis in the submandibular glands of this animal model for cystic fibrosis.
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PMID:The chronically reserpinized rat: decreased glycolytic activity in the submandibular gland. 399 4

A method has been developed for the isolation of outer membranes from Acinetobacter sp. strain MJT/F5/199A. Washed cells were broken in a French press and, after deoxyribonuclease and ribonuclease treatment, removal of intact cells, and four washes in 20 mosmol phosphate buffer, pH 7.4, with centrifugation at 25,000 x g for 10 min, preparations of cell wall fragments from which almost all pieces of plasma membrane had been removed resulted. Treatment of the cell walls with lysozyme and further washing, in the presence of 20 mM MgCl(2), yielded preparations of outer membranes. Electron microscopy of freeze-etched preparations shows that a regular pattern of subunits is present on the outer surfaces of intact cells. After negative staining, these subunits are visible on isolated walls and outer membranes; they can be removed by brief treatment with papain. In section, the cell wall structure is that typical of gram-negative bacteria, but the subunits are not detectable on the surface of the outer membrane. The outer membrane retains the appearance of a "unit membrane" in the cell wall, isolated outer membrane, and papain-treated outer membrane fractions. Both cell walls and outer membranes contain a high percentage of protein (76 and 84%, respectively) and not more than 5% carbohydrate, of which glucose and galactose are constitutents. The outer membranes of this Acinetobacter thus differ in structure and composition from those of bacteria in the Enterobacteriaceae.
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PMID:Isolation of outer membranes with an ordered array of surface subunits from Acinetobacter. 412 37

1. The action of beryllium on the following enzymes has been examined: alkaline phosphatase (Escherichia coli and kidney), acid phosphatase, phosphoprotein phosphatase, apyrase (potato), adenosine triphosphatase (liver nuclei, liver mitochondria, brain microsomes), glucose 6-phosphatase, polysaccharide phosphorylases a and b, phosphoglucomutase, hexokinase, phosphoglyceromutase, ribonuclease, A-esterase (rabbit serum), cholinesterase (horse serum), chymotrypsin. Alkaline phosphatase and phosphoglucomutase are inhibited by 1mum-beryllium sulphate whereas the other enzymes are largely unaffected by 1mm-beryllium sulphate. 2. Possible mechanisms for the inhibition of phosphoglucomutase and alkaline phosphatase are discussed.
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PMID:The inhibition of enzymes by beryllium. 428 87

1. Treatment of washed rat liver microsomes in a medium containing 0.12m-sucrose, 12.5mm-potassium chloride, 2.5mm-magnesium chloride and 25mm-tris-hydrochloric acid buffer, pH7.6, with 2m-lithium chloride at 5 degrees for 16hr. leads to the formation of membranes free of ribosomes and ribosomal subunits. 2. Confirmation of the absence of ribosomes from lithium chloride-prepared membranes was obtained by treatment of the membranes with sodium deoxycholate, followed by sucrose-density-gradient centrifugation, which showed the complete absence of ribosomes. 3. Treatment of membranes with phenol, followed by sucrose-density-gradient analysis of the isolated RNA, showed the presence of a small amount of 4s material. Repetition of the phenol extraction procedure in the presence of liver cell sap as a ribonuclease inhibitor again showed the presence of only 4s material. The 4s RNA was shown to be transfer RNA by the fact that it had the same capacity for accepting (14)C-labelled amino acids as isolated transfer RNA from rat liver pH5 enzyme. 4. Analysis showed that microsomes and membranes possessed similar glucose 6-phosphatase, NADH-2,6-dichlorophenol-indophenol reductase, NADH-neo-tetrazolium reductase, NADH-cytochrome c reductase and ribonuclease activities. 5. (3)H-labelled ribosomal RNA binds to membranes. However, isolation of the bound RNA by the phenol extraction procedure, followed by sucrose-density-gradient analysis, shows the RNA to be degraded to 7s material. Very little breakdown of (3)H-labelled ribosomal RNA bound to membranes occurs if the binding and isolation are carried out in the presence of liver cell sap.
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PMID:Preparation of ribosome-free membranes from rat liver microsomes by means of lithium chloride. 431 14

A method is described for separation of polyribosomes from as few as 25 isolated Islets of Langerhans, representing about 250 mug of pancreatic tissue. Islets are labeled with [(3)H]leucine and polysomes are isolated with liver polyribosomes, which serve as carrier and inhibitor of ribonuclease activity. Islets incubated at 37 degrees C for 45 min in 15.5 mM glucose, then pulsed with [(3)H]leucine, incorporated about 2-3 times more label into nascent peptides on islet polysomes than islets incubated in 2.8 mM glucose. Sucrose gradient analysis of the labeled polysomes indicated that raising the glucose concentration preferentially stimulated synthesis of peptides on trisomes and larger polyribosomes. Islets incubated with [(3)H]leucine for 15 min incorporated two-thirds of the label into proteins on membrane-bound polysomes. At least 85% of the proinsulin synthesis during this time occurs on membrane-bound polysomes.
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PMID:Insulin biosynthesis: studies of Islet polyribosomes (nascent peptides-sucrose gradient analysis-gel filtration). 455 Nov 47

Log-phase Tetrahymena were washed and resuspended in a dilute salt solution supplemented with glucose, acetate, pyruvate, or carmine, as desired, and then incubated for 5 h. Intra- and extracellular activities of acid phosphatase, alpha-glucosidase, and ribonuclease were assayed. Extracellular activities were corrected for proteolytic degradation. The three nutritive substrates affected both the amount and pattern of extracellular enzyme release, but carmine had no effect. Intracellular activities declined early in the starvation period, but partially recovered with time, particularly alpha-glucosidase activity. Acetate reduced the decline in acid phosphatase activity; acetate and glucose enhanced the recovery of alpha-glucosidase activity; carmine had no effect on intracellular enzyme activities. Protein content changed little and was unaffected by the addition of substrates. Glycogen content increased during incubation; acetate and glucose enhanced the increase.
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PMID:Lysosomal physiology in Tetrahymena. I. Effect of glucose, acetate, pyruvate, and carmine on intracellular content and extracellular release of three acid hydrolases. 463 42

Spermatozoa from the cauda of the epididymis of the hamster and rat were incubated with [5-(3)H]uridine and glucose. By using a procedure avoiding bacterial and other cellular contamination, sonic extracts were prepared and digested with deoxyribonuclease and Pronase. Radioactive RNA of high molecular weight was isolated by two methods: (a) gel filtration on Sephadex G-75 columns and (b) polyacrylamide-gel electrophoresis in which it migrated in the region of 28S and 23S RNA markers. The macromolecules were alkali-labile and hydrolysed by ribonuclease. From (3)H radioactivity and E(260) of the isolated RNA the rate of incorporation of uridine into RNA of spermatozoa was calculated to be 0.1-0.5nmol/h per mg of RNA.
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PMID:Ribonucleic acid synthesis by spermatozoa from the rat and hamster. 474 26

1. Mitochondria were isolated from rat liver in a way that kept bacterial contamination at a minimum. 2. The activity of oxidative phosphorylation was unchanged under these conditions, whereas the ability of the preparations to incorporate amino acids into protein was insignificant, though it could be enhanced somewhat by the presence of EDTA. This enhancement was sensitive to ribonuclease. 3. The active time of incorporation did not exceed 15min. at 30 degrees . 4. Microsomal contamination, as measured by glucose 6-phosphatase activity, was about 5%. 5. The ability of isolated bacteria to incorporate amino acids into protein was greatly enhanced by the addition of mitochondria or heat-inactivated mitochondria. 6. A correlation was found between the growth rate of bacteria and the amino acid-incorporating activity. 7. Amino acid incorporation by combined mitochondrial-bacterial systems was inhibited by 2,4-dinitrophenol. 8. The results confirm and extend the earlier findings made in our Laboratory that isolated liver mitochondria, when free from contaminating bacteria and obtained from adult rats, are not able to catalyse the incorporation of amino acids into protein at a measurable rate. 9. The results are discussed with special emphasis on the validity of these findings.
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PMID:A critical study of amino acid incorporation into protein by isolated liver mitochondria from adult rats. 496 94

The distribution of ribonucleases among bacteria has been determined from the examination of a wide variety of species. Bacteria that had been growing rapidly on a solid medium were harvested, treated with acetone and incubated in the presence of EDTA between pH4 and pH9. The ribonuclease activity was determined from the rate at which acid-soluble nucleotides were released. Out of nearly 200 strains examined, about 30 did not contain a detectable ribonuclease. The pH optima of ribonucleases in the remainder were sufficiently distinctive to suggest a use in taxonomy. Escherichia coli B was examined in more detail to determine the factors responsible for variations in the ribonuclease content of this bacterium. Growth rate had little influence on ribonuclease content when a complex medium containing no readily assimilable carbohydrate was used; the addition of glucose resulted in a marked increase in ribonuclease and a dependence of enzyme content on growth rate. An increase in the concentration of sodium chloride in the medium decreased the ribonuclease content of bacteria growing on it.
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PMID:Magnesium ion-independent ribonucleic acid depolymerases in bacteria. 533 80


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