Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.27.1 (RNase)
 16,360 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Optimal assay conditions are described for 8 hydrolases of Euglena gracilis var. bacillaris, SM-L1 (streptomycin-bleached) strain, 7 of which have an acid pH-optimum. Acid-phosphatase, beta-galactosidase, beta-glucosidase, b-fucosidase, cathepsin D, RNase, DNase, and an esterase are active in cell homogenates. Amylase has very low activity, and beta-glucuronidase, arylsulfatase, beta, N-acetyl-glucosaminidase, alpha-fucosidase, and alpha- and beta-mannosidase are inactive.
 ...
PMID:Hydrolytic enzymes of Euglena gracilis: characterization and activity as a function of culture age and carbon deprivation. 0 4

Cytochemical methods are used to examine the distribution and localization of acid phosphatase, non-specific esterase, ribonuclease and peroxidase activity in the walls of the spores of the heterosporous Marsileaceae before and during germination. In the quiescent spore, the principal activity is associated with the perine layer of the wall and the intine, with some activity in the outer, gelatinous wall layer, but none in the exine. The microspores of Marsilea and Pilularia have non-specific esterase activity concentrated in the intine inthe immediate vicinity of the germinal site; that is, above the position of the future male gametangia. The enzymes are not leached from the wall during hydration of the spores, although ribonuclease is redistributed during imbibition with a high concentration of activity remaining in or around the germinal site. The wall enzymes occur together with PAS-reactive and acidic carbohydrates, lipids, and in the microspore perine, beta-lectins. Following the enzyme pattern, the beta-lectins are found to be concentrated in the region of the germinal site. beta-Lectin activity is absent from the megaspore wall. Acidic carbohydrates are confined to the gelatinous wall layer and this layer also binds concanavalin A. In contrast to what has been found for other plant cells, the spore-wall beta-lectins are not water-labile; the activity is not significantly diminished after hydration. This surprising stability suggests that these molecules, together with the enzymes, may be retained in position in the wall by the waterproof overlay of lipid. From the evidence of preliminary developmental studies, it appears that the enzymes associated with the perine layer of the wall originate in the sporophytic tapetal periplasmodium and inclusion of the activity is concurrent with wall differentiation, while the activity associated with the intine is derived from the gametophyte. It is possible, however, in the megaspore at least, that the distribution of the activity may to some extent be influenced by a system of exine channels which communicates between the two domains of the wall during sporogenesis. No definite information is obtained concerning the utility of the enzymes and associated molecules in the life of the spore. Acting separately or in co-operation, their role could conceivably be connected with one or more of four processes; wall differentiation, gametophyte nutrition, gametophyte protection or reproduction. Each of these possibilities is discussed.
 ...
PMID:Developmental mechanisms in heterospory: cytochemical demonstration of spore-wall enzymes associated with beta-lectins, polysaccharides and lipids in water ferns. 52 75

The enzymes from the venom of Heterometrus scaber, the indole compounds present and the toxic protein of the venom have been studied. The venom contains acid phosphatase, ribonuclease, 5'-nucleotidase, hyaluronidase, acetylcholine esterase and phospholipase. A. The indole compounds present in the venom have been identified as 5-hydroxytryptophan, tryptophan, serotonin and tryptamine, along with two unidentified indole compounds. The venom produces hyperglycaemia in sublethal doses and this has been found to be due to increased adrenaline secretion. The toxic protein of the venom has been obtained in a pure form by (NH4)2SO4 fractionation, followed by fractional precipitation with acetone and chromatography over DEAE-Sephadex. The toxic fraction has been found to be homogeneous on acrylamide gel electrophoresis. It is a glycoprotein (molecular weight 15 000) containing 1.74% glucosamine, 0.87% galactosamine, 0.313% sialic acid, 3.25% fucose and 0.45% of an unidentified neutral sugar. It did not show any enzyme activities, haemolytic activity or inhibition of succinate dehydrogenase activity but it produced hyperglycaemia in sublethal doses. The toxic level (intravenous administration in rats) was found to be 0.72 mg/kg body weight.
 ...
PMID:Investigations on the venom of the South Indian scorpion Heterometrus scaber. 111 82

In addition to previous taxonomic work, eight biochemical tests have been applied to the study of 580 Bacillus strains belonging to 22 species. The attack of chitin, melibiose and amygdalin can be used for the differentiation of some species. It is the same with most of the enzymes studied here, although Tween-esterase and DNase are often present in the majority of the isolates. RNase is still more frequent, being found in nearly all the strains. On the other hand, arginin-dihydrolase appears to be very rare and ornithin-decarboxylase seems always absent.
 ...
PMID:[Interest of some additional biochemical tests for the classification of "Bacillus" (author's transl)]. 119 Jun 35

A comparative enzyme analysis was performed on 3 pancreatic extracts generally used for dermal-epidermal separation, namely, crude trypsin (Difco), crude trypsin (Sigma) and pancreatin. A fourth pancreatic extract, crude lipase, was subjected to a corresponding analysis. The 4 extracts were assayed for activities of: protease (total), trypsin, chymotrypsin, carboxypeptidase-A, amylase, elastase, lipase, esterase, arylesterase and ribonuclease. Relative activities of the different proteolytic enzymes were individualized by utilizing specific inhibitors. Insignificant differences were observed between the enzyme activities of crude trypsin (Difco) and pancreatin. Crude lipase displayed similar enzyme activities as these two extracts in addition to high lipolytic, esterolytic and arylesterolytic activities. Crude trypsin (Sigma) exhibited higher tryptic and chymotryptic activities than the other extracts but lacked all further enzyme activities. Epidermal separation was performed using similar incubation conditions for each extract and skin from the same donor. Ultrastructural examination of the detached epidermis revealed that a more effective separation could be achieved by crude lipase.
 ...
PMID:An analysis of pancreatic enzymes used in epidermal separation. 123 61

1. The response to thermal acclimation of five key rate-limiting enzymes of intermediary metabolism and of six degradative enzymes was measured in tissue extracts of adult Drosophila melanogaster which had been acclimated for 4 days to 15, 25 or 30 degrees C. 2. Three enzymes of intermediary metabolism (HK, alpha-GPDH and CO) showed positive thermal compensation, which is the type of response characteristic of the enzymes involved in energy metabolism in vertebrate ectotherms. 3. The data obtained for CS and G6PDH showed no evidence for increased activity of TCA cycle nor of the pentose phosphate pathway upon cold acclimation in D. melanogaster. 4. Two degradative enzymes, ADH and non-specific esterase, showed inverse thermal compensation which is the type of response characteristic of degradative enzymes in vertebrate ectotherms. 5. In contrast to the situation in vertebrate ectotherms, catalase and the three lysosomal enzymes assayed (APH, acid DNase and acid RNase) displayed positive rather than inverse compensation. 6. The results presented here extend the data on the range of D. melanogaster enzymes which show compensation upon thermal acclimation and on the type of acclimation response which occurs.
 ...
PMID:The effect of acclimation temperature on enzyme activity in Drosophila melanogaster. 165 Dec 3

Intradermal injection of MY-1, a nucleic acid fraction extracted from Mycobacterium bovis strain BCG, induced in situ infiltration of mononuclear cells, most of which were asialo GM1 (GA1)-positive as determined by immunofluorescence microscopy. The infiltration occurred with as little as 1 microgram of MY-1 and lasted for a week. Double immunofluorescence microscopy revealed that the infiltrating GA1-positive cells were all positive for Ly-5, and partially positive for Thy-1.2, but negative for Mac-1, Ia, mu-chain, Lyt-1, Lyt-2, L3T4, and Fc receptor II. They contained neither peroxidase nor nonspecific esterase. The infiltrating cells thus markedly resembled natural killer (NK) cells in their cytochemical characteristics and surface markers. DNase and RNase destroyed the GA1-positive cell-inducing activity of MY-1. These results indicate that the nucleic acid components of MY-1 are responsible for this effect.
 ...
PMID:In situ infiltration of natural killer-like cells induced by intradermal injection of the nucleic acid fraction from BCG. 248 May 10

Gabonase, an enzyme which acts on fibrinogen and factor XIII in uniquely thrombin-like ways, was purified to electrophoretic homogeneity from the venom of Bitis gabonica. On sodium dodecyl sulfate-polyacrylamide electrophoresis, the reduced protein behaved as a single chain with Mr = 30,600. The enzyme contains 20.6% carbohydrate, no free sulfhydryl groups and hence, from amino acid analysis, five disulfide bonds. Its extinction coefficient (E1%1cm) at 280 nm is 9.6. Its pI is 5.3. Gabonase has an active serine residue, is inactivated by phenylmethanesulfonyl fluoride, and has an active histidine which reacts with the chloromethyl ketone of tosyl-L-lysine. Its NH2-terminal amino acid sequence (Val-Val-Gly-Gly-Ala-Glu-Cys-Lys-Ile-Asp-Gly-His-Arg-Cys-Leu-Ala-Leu-Leu -Tyr-) is homologous to the B chain of thrombin. The activity of the enzyme is stabilized by calcium ion. It exhibits strong N alpha-p-tosyl-L-arginine methyl esterase activity, hydrolyzes tripeptide nitroanilide derivatives weakly or not at all, and cleaves no peptide bonds in insulin, glucagon, or the S peptide of ribonuclease. Gabonase clots fibrinogen with a specific activity of 45 NIH thrombin-equivalent units/mg, releasing both fibrinopeptides A and B and showing substrate inhibition at fibrinogen concentrations of 3 mg/ml or greater. The enzyme also activates factor XIII. It is not inactivated by either heparin or hirudin.
 ...
PMID:Thrombin-like enzyme from the venom of Bitis gabonica. Purification, properties, and coagulant actions. 352 80

The present study was undertaken to elucidate further the enzymatic changes in dystrophic muscle using multivariate analysis. The activities of 14 kinds of enzymes, including 6 exopeptidases, 4 endopeptidases, beta-N-acetyl-D-glucosaminidase, phosphatase, esterase, and ribonuclease, were examined in forelimb and hindlimb muscles as well as in cardiac muscle of dystrophic mice and their controls. Two principal components identified from the enzymatic spectrum proved to be related especially to aminopeptidases and to serine proteinases, respectively. The enzymatic changes in forelimb muscle were very similar to those in hindlimb muscle when both were compared to those in cardiac muscle. The changes in aminopeptidases were unique to the limb muscles, whereas those of serine proteinases were unique to cardiac muscle of dystrophic mice. In the future, more attention should be focused on the role of exopeptidases in pathogenetic mechanisms of muscular dystrophy, because of the possibility that they play a major role in the initial stage of muscular dystrophy.
 ...
PMID:A multivariate study on enzymatic changes in limb muscles and heart muscle of dystrophic mice. 367 74

One hundred twenty-seven isolates of Aeromonas comprising the three currently recognizable species (A. hydrophila, A. sobria, and A. caviae) were evaluated for biochemical and exoenzymatic properties. Aeromonas species were generally (greater than 90%) characterized as gram-negative fermentative rods that were oxidase-, catalase-, and beta-galactosidase-positive, produced arginine dihydrolase, and failed to decarboxylate ornithine. More than 95% of all isolates tested failed to grow on 6.5% salt or thiosulfate-citrate bile salts agar and were resistant to the vibriostatic agent 0/129. Most Aeromonas species produced acid from hexoses while failing to ferment alcoholic sugars or trisaccharides. In exoenzymatic studies, Aeromonas species were uniformly found to produce several exoenzymes, including amylase, DNase, RNase, esterase, lipase, gelatinase, protease, fibrinolysin, and chitinase. Within the genus, a number of biochemical and enzymatic properties were found to be associated with one or more of the taxonomically recognizable species. These properties included glycoside utilization, Heiberg grouping based upon fermentation of arabinose, sucrose, and mannose, and the elaboration of several extracellular enzymes (elastase, hemolysin, lecithinase, phosphatase). In addition, phenotypic markers previously associated with enterotoxigenic Aeromonas isolates were almost exclusively found among A. hydrophila and A. sobria species, suggesting that these species are the major enteric pathogens.
 ...
PMID:Biochemical and exoenzymatic properties of Aeromonas species. 388 8


1 2 3 4 Next >>