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:3.1.27.5 (RNase)
17,967 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The ultrastructural study of liver tissues from 38 patients with type B viral hepatitis consistently showed the presence of hepatitis B core antigen of 21-25 nm size in the liver cell nuclei and to a lesser extent in the cytoplasm. This finding and the demonstration of the tubular form of hepatitis B surface antigen in the proliferative degranulated endoplasmic reticulum constituted the etiologic criterion for the diagnosis of the disease. The double-shelled Dane-like particles were frequently found in association with the tubular form of the surface antigen. The core particles were found in the protoplasmic processes of hepatocytes and this correlated with the immunofluorescent microscopic findings that the antigen may be shed into circulation with the protoplasm. The core antigen was found to resist digestion by various enzymes such as protease, DNase, RNase, phospholipase C, lipase, lysozyme, diastase, neuraminidase and hyaluronidase, all of which did not destroy the immunoreactivity as demonstrated by immunoelectron and immunofluorescent microscopy. Similarly, sodium dodecyl sulfate, Tween 80 and mercaptoethanol also had no effect. The formalin-fixed paraffin-embedded liver tissue sections could be treated with protease to facilitate the immunofluorescent staining for the core antigen in tissue.
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PMID:Structural and immunoreactive characteristics of hepatitis B core antigen. 5 6

Lipoprotein lipase was purified from bovine milk and labeled with 125I. After intravenous injection to rats the labeled lipase rapidly disappeared from the blood. The initial half-life was about 1 min and more than 70% of the radioactivity was found in the liver at 10 min. 30 min after the injection about 10% of the injected radioactivity was present in acid-soluble form in blood, indicating that the enzyme had been rapidly degraded. Injection of asialofetuin, ribonuclease B or mannan in amounts known to block the hepatic receptors for glycoproteins with exposed galactose, N-acetylglucosamine or mannose residues did not retard the removal of the lipoprotein lipase. Thus, some other, as yet undefined, receptor is implicated. Lipoprotein lipase is known to bind to heparin and some related polysacchrides. Heparin injected before the enzyme delayed its removal and heparin injected after the enzyme caused an immediate increase in blood radioactivity, signifying return from tissues to blood of labeled enzyme. Lipoprotein lipase is present at the endothelium in several extrahepatic tissues and is rapidly turned over. Its presence in blood in appreciable amounts would cause a derangement of lipid transport. The efficient hepatic removal of the enzyme may thus serve an important physiological purpose in keeping the blood levels of this enzyme low.
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PMID:Rapid removal to the liver of intravenously injected lipoprotein lipase. 9 43

On the basis of morphological and biochemical differences, the exocrine pancreatic tissue has been divided in peri- and teleinsular regions. In the present study the enzymatic profile of these regions has been investigated by the immunofluorescent technique using antibodies against nine pancreatic enzymes (alpha-amylase, lipase, chymotrypsinogen A, trypsinogen, elastase, carboxypeptidase A and B, DNase and RNase A). These antibodies were specific to their antigens without cross reaction. By immunofluorescence, most acinar cells of the normal rat pancreas were positive to the nine enzymes tested. However, an inhomogeneity in the staining pattern was found; specifically, the cells located in the periinsular region of many islets showed a brighter fluorescence than acinar cells in the teleinsular tissue. These data add a new parameter to describe the inhomogeneity of the exocrine pancreas.
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PMID:Immunohistochemical localization of exocrine enzymes in normal rat pancreas. 11 Aug 72

The ascites form of a chemically induced guinea pig hepatoma, line-10, was resistant to killing in vitro by xenogeneic antibody and guinea pig complement. Pretreatment of line-10 cells with certain proteolytic enzymes rendered tham susceptible to the killing action of antibody and guinea pig complement. The effects of enzyme pretreatment were dependent on enzyme concentration, temperature, and could be blocked by addition of competitive or non-competitive inhibitors. The effect of the enzyme treatment could reversed by incubating the treated cells at 37 degrees C (but not at 0 degrees C), in the absence of the enzyme. Effective enzymes included ficin, bromelain, pronase, elastase, papain, trypsin, collagenase, lipases type I and type VI, and the neuraminidase preparation isolated from Clostridium perfringens. The activity of the lipase preparations and the neuraminidase preparation isolated from Clostridium perfringens appeared to be caused by proteolytic enzyme contamination. Enzyme preparations that proved ineffecitve in rendering the line-10 cells sensitive to killing by antibody and guinea pig complement included DNase, RNase, beta-glucuronidase type 6A or type B10, hyaluronidase type V or type VI, and pectinesterase.
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PMID:Lysis of tumor cells by antibody and complement. VI. Enhanced killing of enzyme-pretreated tumor cells. 17 70

The bacteriocin produced by Mycobacterium smegmatis ATCC 14468 was isolated, and a study was made of its chemical, physical, and biological properties. No appreciable bacteriocin activity was found in the culture supernatant fluids, but it was released in appreciable quantities after disruption of the cells. The material was purified 49-fold by means of chromatography on diethylaminoethyl-cellulose, ammonium sulfate fractionation, gel filtration on Sephadex G-200, and chromatography on diethylaminoethyl-Sephadex A-50. Its molecular weight was determined to be approximately 75,000 from the elution profile on Sephadex G-200 chromatography. The bacteriocin was resistant to deoxyribonuclease, ribonuclease, lipase, ultraviolet irradiation, and freeze-thawing, whereas it was relatively less thermostable and was sensitive to proteolytic enzymes. The lethal effect of the bacteriocin was demonstrated by the decrease in viable counts of the bacteriocin-sensitive indicator strain, M. diernhoferi ATCC 19340. The bacteriocin preparation inhibited the growth of HeLa-S3 cells.
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PMID:Purification, properties, and cytotoxic effect of a bacteriocin from Mycobacterium smegmatis. 46 82

Solid media were used to determine which extracellular hydrolytic enzymes are produced by Phytophthora parasitica; P. parasitica var. nicotianae, races 0, 1, and 3; and several other Phytophthora spp. Most isolates produced RNase, DNase, phosphatase, lipase, and cellulase uniformly. All race 3 isolates of P. parasitica var. nicotianae exhibited protease activity on a medium containing gelatin, while only 33 and 60% of the race 0 and 1 isolates, respectively, and 14% of the P. parasitica isolates did so. Addition of sorbose to this medium enabled the detection of protease activity by most of the isolates. Amylase activity, measured in the culture fluid, was higher in race 3 than in races 0 or 1 of P. parasitica var. nicotianae and P. parasitica.
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PMID:An examination of enzyme production of Phytophthora spp. on solid and liquid media. 75 80

A substance which inhibits brain formation in decapitated regenerating planarians (Dugesia etrusca) was characterized and partially purified. The substance's inhibitory activity was followed during each purification procedure by adding freshly decapitated animals of a standard size to each fraction, and later measuring the resultant regenerated brain volume. The inhibitory activity remained in the supernatant after a 10000 g centrifugation of a cell-free homogenate. Most of the activity sedimented when the 10000 g supernatant was centrifuged at 32000 g. The degree of inhibitory activity increased with increased numbers of animals in the initial homogenate. The substance has an apparent molecular weight between 2 X 10(5) and 4 X 10(5) daltons. Digestion by pronase destroyed the activity, but treatment with RNase, DNase I, or lipase had no significant effect. The inhibiting substance has an isoelectric point (pI) of between 4-75 and 5-38 and migrates to the anode when electrophorezed in pH 6-8 buffer.
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PMID:Characterization of an organ-specific differentiator substance in the planarian Dugesia etrusca. 87 May 91

A strain of Actinomyces odontolyticus, originally isolated from human dental plaque, produced a non-dialyzable, trypsin-sensitive substance that was bactericidal for certain strains of bifidobacteria at 42 degrees C but not at 37 degrees C. Detectable quantities of the bacteriocin were not produced in liquid media. Experimentally useful yields were obtained by extraction from pour plate cultures of producer cells. At 42 degrees C, exponential killing did not occur until indicator cells had doubled at least once. At 37 degrees C, the bacteriocin effected a transient bacteriostasis. Partially purified concentrates were obtained by diethylaminoethyl-cellulose chromatography, and such material was not inactivated by ribonuclease, deoxyribonuclease, or lipase. Pronase, trypsin, and exposure to 100 degrees C for 20 min completely abolished activity. Inhibitory activity was considerably reduced by exposure to a pH of either 3 or 11. Treatment of producer cells with curing agents did not induce a high frequency of non-bacteriocinogenic cells. The odontolyticin was adsorbed by susceptible, as well as resistant, bacteria.
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PMID:Bacteriocin from Actinomyces odontolyticus with temperature-dependent killing properties. 90 31

The binding of taurodeoxycholate to pancreatic lipase and a few other proteins has been studied with equilibrium dialysis and in gel filtration experiments. A three compartment dialysis cell has been used; with this cell, complete equilibration is not necessary for calculation of the binding even at bile salt concentrations above the critical micellar concentration. The results indicate that taurodeoxycholate does not bind to lipase below the critical micellar concentration, that the binding starts in the critical micellar concentration range of the bile salt and reaches around 12 mol taurodeoxycholate per mol of lipase at taurodeoxycholate concentrations well above the critical micellar concentration. Previous results indicating a binding of maximally 1-2 mol taurodeoxycholate/mol lipase were too low, depending on the experimental conditions in which complete equilibration was not obtained. The binding isotherm for taurodeoxycholate to lipase is similar to that for co-lipase; colipase and lipase in mixture bind as much taurodeoxycholate as the sum for the single proteins. Taurodeoxycholate binds to ribonuclease and chymotrypsinogen to a similar extent as to lipase.
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PMID:On the binding of bile salt to pancreatic lipase. 100 92

An in vitro system of guinea pig pancreatic lobules convenient for the study of secretory processes is described in this paper. In this system: (a) the over-all glandular architecture of the tissue is preserved: lobules remain morphologically intact through 5 hours; (b) amylase discharge from unstimulated lobules is low (similar to 4%/hour) and linear over the 5 hours tested; (c) response to carbamylcholine chloride (10-5 M) is energy-dependent, rapid, and extensive (92% discharge of amylase by 5 hours); (d) initial rates of discharge remain stable over the first 3 hours; and (e) no autoactivation of zymogens occurs in incubation medium or tissue. The activation of four zymogens, i.e. chymotrypsinogen, trypsinogen, and procarboxypeptidases A and B, was studied using the following criteria for optimal activation: (a) maximal activation attainable under experimental conditions; (b) stability at the level of maximal activation; and (c) linear relationship between amounts of protein activated and enzyme activity elicited by activation. The concentration of activators (trypsin or enterokinase) and secretory protein, the presence or agents (bovine plasma albumin or Triton X-100) which minimize adsorptive losses of secretory protein on glass or plastic surfaces, and the temperature at which activation is carried out were found to be critical and different for each of the zymogens tested. The kinetics of the appearance of three enzyme activities (amylase, lipase, and ribonuclease) and four potential proteolytic activities (chymotrypsinogen, trypsinogen, and procarboxypeptidases A and B) into the incubation medium was studied under different conditions; i.e. rest and stimulation with various secretogogues (carbamylcholine chloride, caerulein, and pancreozymin). All seven activities estimated to represent similar to 75% of the secretory protein output of the exocrine pancreas were discharged in synchrony and in constant proportions and were released from the tissue to the same extent under each experimental condition investigated.
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PMID:Studies on the guinea pig pancreas. Parallel discharge of exocrine enzyme activities. 112 25


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