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 following enzymatic activities were measured in serum of patients with benign and malignant ovarian tumors before treatment: alkaline and acid phosphatases, aspartyl (AspAT) and alanyl (AlAT) aminotransferases, leucyl (LAP) and alanyl (AAP) aminopeptidases, lactate dehydrogenase (LDH), gamma-glutamyl transpeptidase, cathepsin, alkaline ribonuclease (RNase) and beta-glucuronidase. It was shown that at least three determinations (phosphatases and LAP) are practically useless in a discrimination between the examined groups. RNase in combination with AspAT (AlAT) or RNase with AAP and LDH were found to give the best results as marker enzymes.
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PMID:Serum enzymes in ovarian carcinoma. 4 48

The activity of certain enzymes of energy metabolism (cytochrome c oxidase, citrate synthase, malate dehydrogenase, and lactate dehydrogenase) and of lysosomes (beta-glucuronidase, beta-N-acetylglucosamindase, arylsuphatase, ribonuclease, deoxyribonuclease, acid phosphatase, and cathepsin D) was assayed from m. rectus femoris of mice trained 5 days per week, 1 hr per day for 4 weeks according to 4 different programmes: I. running speed 20 m/min, horizontal track, II. 25 m/min, horizontal track, III. 20 m/min 8 degrees uphill inclination, and IV. 25 m/min 8 degrees uphill inclination. Oxidative capacity increased and anaerobic capacity decreased without distinction between the different traning programmes. Of acid hydrolases assayed the activities of beta-glucuronidase and cathepsin D were increased independently of training intensity. Simultaneous histochemical observations on beta-glucuronidase and arylsulphatase activities in the contralateral m. rectus femoris showed more intense staining in red as compared to white muscle fibres. It is suggested that training affected the red fibres and that the applied level of loading was probably too low to cause major involvement of white fibres.
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PMID:Oxidative and lysosomal capacity in skeletal muscle of mice after endurance training of different intensities. 21 99

The traditional ligature methods were added with freezing of the left hepatic lobe resection line in order to block up parenchymatous bleeding and cholerhagia in atypical resection of the liver. Alterations in the enzymatic activity (alaninic and asparaginic transaminases alkaline phosphotase, lactate dehydrogenase and ribonuclease) in the blood serum and liver of the rabbits allowed to judge about the character of inflammatory and destructive changes in the liver following the use of the abovementioned methods. The rise of the activity of the enzymes under study within the first days after operation and its normalization by the 7th to 14th days in all the studied variants of hemo- an cholestasis have been established.
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PMID:[Effectiveness of cryogenic action in experimental liver resection]. 44 32

The previous reports of inhibition of alcohol dehydrogenase and lactate dehydrogenase by the vitamin folic acid and its analogues are in error. The high absorbance of solutions containing folate causes distortion of the measurements of reaction velocities, leading to apparent inhibitions. When cuvettes of sufficiently short optical path length are used, no inhibition by folate can be observed. Similarly, the reported inhibition of ribonuclease by folate is an artifact. Glutamate dehydrogenase and dihydropterin reductase actually are inhibited by folate. The reported nonspecific inhibitions of over a dozen enzymes by folate, though, must be regarded as erroneous.
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PMID:Nonspecific inhibition of dehydrogenases by folates: an artifact. 50 60

It is shown that the method proposed by Baker and Isenberg [Biochemistry, 15, 629 (1976)] for estimating secondary structure composition of proteins from circular dichroic spectra is a least-squares fitting technique. Estimates obtained by this method for myoglobin, lysozyme, lactate dehydrogenase, papain, and ribonuclease are not substantively different from those obtained using unconstrained linear least squares.
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PMID:Least-squares analysis of circular dichroic spectra of proteins. 85 60

The hydroxyl groups of poly(ethyleneglycol) have been esterified (partly) with a number of carboxylic acids. When these esters are included in dextranpoly(ethyleneglycol)-water biphasic systems the partitions of proteins and membranes between the two phases (and the interface) are in some cases strongly affected. The affinity of serum albumin for the poly(ethyleneglycol)-rich phase is strongly increased when the fatty acid group consists of more than 10 carbon atoms. The partition also depends on the number of double bonds in the fatty acid. A corresponding relationship is found for membranes from spinach chloroplasts. The partitions of ovalbumin, lysozyme (EC 3.2.1.17) and ribonuclease (EC 3.1.4.22) are not influenced by the fatty acid esters. Esters of dibasic carboxylic acids show a minute but marked effect on the partition of proteins in general while malate and tartrate esters affect strongly the partition of chloroplast membranes. The partitions of both proteins and membranes are influenced by poly(ethyleneglycol) deoxycholate. Experiments with malate dehydrogenase (EC 1.1.1.37), lactate dehydrogenase (EC 1.1.1.27), fumarase (EC 4.2.1.2), enolase (EC 4.2.1.11) and glutamate-ocaloacetate transaminase (EC 2.6.1.1) show that their partitions, measured on enzymic activity basis, is changed when esters of benzoic, linolenic, tartaric or deoxycholic acid are included in the biphasic system. The mechanism behind the effect of the esterified poly (ethyleneglycol) on the partition of biomaterial, in this type of aqueous biphasic systems, is discussed in terms of a direct binding of the esters to the partitioned material.
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PMID:The effect of poly(ethyleneglycol) esters on the partition of proteins and fragmented membranes in aqueous biphasic systems. 99 68

The hydrophobic nature of proteins is characterized by a degree of 2-p-toluidinonaphthalene-6-sulphonate (TNS) affinity to them and is pronounced quantitatively in the semi-saturated (C1/2) concentrations. This index correlates directly with the position of TNS emission maximum after the binding with proteins and reversely with the yield of fluorescence. The preparations of phosphofructokinase, lactate dehydrogenase, xantinoxidase, glyceratekinase, lysozyme, RNase during the long (1-2 h) contact with TNS change the values C1/2, that evidences for interaction with the hydrophobic indicator of new structures of protein molecule or for a change in the nature of its linkage itself. An attempt is made to characterize the accessible for TNS hydrophobic nature of individual proteins by a coefficient of molar hydrophobic nature which unites three mentioned characteristics. Serum albumin, insulin, glucogon, alpha chemotrypsin, DNase are most hydrophobic, pyruvate kinase, aldolase, urease, RNase--least hydrophobic, Glycerate kinase, pyruvate decarboxylase, phosphofructokinase, lactate dehydrogenase, alcohol dehydrogenase, xanthinoxidase, trypsin, lysozyme are in intermediate position.
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PMID:[Comparative characteristics of hydrophobic nature of certain proteins by their interaction with 2-p-toluidinonaphthalene-6-sulfonates]. 120 4

Progressive changes in myosin isozyme expression and in energy-generating enzyme activities were followed in the diaphragm and, for comparison, in axial and appendicular muscles of rats from 18 d gestation to maturity. Native myosins were characterized by pyrophosphate gel electrophoresis. Myosin heavy-chain (MHC) isozymes were measured with ELISA using monoclonal antibodies and were localized by immunocytochemistry. RNA transcripts for the MHCs were demonstrated on Northern blots and by RNase protection assays. Quantitative activities of malate dehydrogenase (MDH), beta-hydroxyacyl CoA dehydrogenase (beta OAC), 1-phosphofructokinase (PFK), lactate dehydrogenase (LDH), creatine kinase (CK), and adenylokinase (AK) were measured in muscle homogenates and in individual fibers by fluorometric pyridine nucleotide-dependent assays. Compared to limb muscles, expression of neonatal myosin in the diaphragm is precocious. Neonatal MHC mRNA is prominent in the diaphragm at 19 d gestation, and neonatal myosin is the major MHC isoform present at birth. Slow and fast IIa MHCs are also present at birth. Transcripts for IIa MHC are detectable in the diaphragm at 21 d gestation and are upregulated at birth. Comparable signal for IIa MHC mRNA is not found in the gastrocnemius until 10 d postpartum. Adult fast IIb MHC mRNA was detected only as a faint signal at 30-40 d in the diaphragm and then disappeared. Results indicate that a separate phenotype, the IIx type, matures late in diaphragmatic development. The activities of enzymes representing all of the major energy pathways are higher in the fetal diaphragm than in the fetal hindlimb muscles. For example, beta OAC had sixfold higher activity in the diaphragm than in the extensor digitorum longus (EDL) muscle at birth, activity in the diaphragm than in the extensor digitorum longus (EDL) muscle at birth.
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PMID:Metabolic and contractile protein expression in developing rat diaphragm muscle. 202 44

Hepatic ethanol metabolism generates the reactive intermediate, acetaldehyde, which binds to proteins. The binding of acetaldehyde to purified enzymes was determined in order to ascertain whether such binding altered their catalytic functions. [14C]Acetaldehyde was incubated with alcohol dehydrogenase, glucose-6-phosphate dehydrogenase, lactate dehydrogenase and RNase A, each at 37 degrees C (pH 7.4). In some reactions, sodium cyanoborohydride was included for stabilization of Schiff bases, formed as a result of the reaction between acetaldehyde and the amino groups of the enzymes. Portions of each reaction mixture were removed for determination of stable and total (stable plus borohydride-reducible) adducts. Alcohol dehydrogenase and lactate dehydrogenase were not inhibited by adduct formation. Glucose-6-phosphate dehydrogenase and RNase, the activities of which depend on a lysine residue at their catalytic sites, were inhibited in a dose- and time-dependent manner. The degree of inhibition directly correlated with total adduct formation. Phosphate, known to inhibit binding to the active site lysine of RNase, prevented the inhibition of catalytic activity caused by adduct formation. These findings indicate that the binding of acetaldehyde to lysine at the catalytic site can inhibit enzyme activity.
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PMID:Covalent binding of acetaldehyde selectively inhibits the catalytic activity of lysine-dependent enzymes. 293 8

Isolated pancreatic acini from streptozocin-induced diabetic rats were used to study the role of insulin on the synthesis of specific cellular proteins. When acini were incubated with 0-100 nM insulin for 2 h and then pulsed with [35S]methionine, a dose-dependent increase in [35S]methionine incorporation into total cellular proteins was observed. When acinar cell lysates were subjected to gel electrophoresis, 12 major newly synthesized protein bands were resolved. Insulin (100 nM) increased the incorporation of [35S]methionine into all bands but with significantly different rates, varying from 84 to 216% of control. Next, specific antibodies to amylase, trypsin, ribonuclease, myosin, and lactate dehydrogenase (LDH) were used to evaluate the biosynthesis of known proteins. Insulin stimulated labeled amino acid incorporation into amylase by 148% over control. Insulin stimulated the synthesis of trypsinogen to a similar degree, but ribonuclease synthesis showed a significantly smaller increase of 53% over control. Insulin stimulated myosin and LDH synthesis by 169 and 184%, respectively. A differential pattern of protein synthesis was also observed when acini were treated with two other stimulators of protein synthesis, cholecystokinin and hemin. Both of these stimulators had a reduced effect on ribonuclease synthesis compared with amylase and trypsinogen synthesis but failed to increase myosin synthesis. When the RNAs extracted from control acini and acini treated with 100 nM insulin were translated in vitro, the proteins synthesized were quantitatively similar. This study therefore indicates that insulin has translational effects on acinar protein synthesis, and these effects are nonparallel for various specific acinar cell proteins.
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PMID:Insulin and other stimulants have nonparallel translational effects on protein synthesis. 330 74


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