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)

Haematoxylin-Basic fuchsin-Picric acid (HBFP) technique characterises two varieties of nuclear population in the rat hepatocytes. HBFP technique is capricious and the differentiation step should be controlled stringently; ethanolic picric acid, therefore, is recommended as a differentiation fluid. On the basis of controls treated with (1) ribonuclease (RNase), (2) deoxyribonuclease (DNase), (3) Bouins fluid or (4) protease, this study has determined that DNA-associated protein(s) and some DNA may be responsible for the HBFP produced nuclear fuchsinorrhagia. The heterogeneous nuclei of the rat hepatocytes were statistically analyzed in periportal, centrilobular and intermediate areas. Fuchsinorrhagic nuclei were preponderant in the periportal areas.
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PMID:On the mechanism of HBFP stain and an analysis of heterogeneous nuclei in rat hepatocytes. 9 26

Two low-molecular-weight basic proteins, termed A and B proteins, comprise about 15% of the protein of dormant spores of Bacillus megaterium. Irradiation of intact dormant spores with ultraviolet light results in covalent cross-linking of the A and B proteins to other spore macromolecules. The cross-linked A and B proteins are precipitated by ethanol and can be solubilized by treatment with deoxyribonuclease (75%) or ribonuclease (25%). Irradiation of complexes formed in vitro between deoxyribonucleic acid (DNA) or ribonucleic acid and a mixture of the low-molecular-weight basic proteins from spores also resulted in cross-linking of A and B proteins to nucleic acids. The dose-response curves for formation of covalent cross-links were similar for irradiation of both a protein-DNA complex in vitro and intact spores. However, if irradiation was carried out in vitro under conditions where DNA-protein complexes were disrupted, no covalent cross-links were formed. These data suggest that significant amounts of the low-molecular-weight basic proteins unique to bacterial spores are associated with spore DNA in vivo.
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PMID:Localization of low-molecular-weight basic proteins in Bacillus megaterium spores by cross-linking with ultraviolet light. 11 Jul 90

Antiserum to a purified type R lipopolysaccharide antigen isolated from Neisseria gonorrhoeae was used in a slide agglutination test and compared with conventional carbohydrate utilization and fluorescent antibody tests to confirm the identity of laboratory cultures classified as typical or "atypical" N. gonorrhoeae. Cultures of Corynebacterium vaginalis, N. meningitidis, N. catarrhalis, N. sicca, and N. lactamicus were also tested in the slide agglutination procedure. The addition of both deoxyribonuclease and ribonuclease (1 mg/ml) to the cell suspension medium of phosphate-buffered saline improved the sensitivity and specificity of the agglutination reaction for N. gonorrhoeae. Problems relating to the agglutination test as an aid in identification of N. gonorrhoeae are discussed.
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PMID:Nuclease enhancement of specific cell agglutination in a serodiagnostic test for Neisseria gonorrhoeae. 11 Aug 30

Dipolid human fibroblast-rich tissues contain a macromolecule with a molecular weight between 30,000 and 50,000 daltons which will inhibit the proliferation of fibroblasts in the G1 phase of the cell cycle (i.e., inhibit both 3H-thymidine uptake as well as the normal increase in cell number). The inhibitor is destroyed by trypsin but not by ribonuclease or deoxyribonuclease, and it is thermolabile. It has an acid IEP. It is not cytotoxic, and its inhibitory activity appears to be completely reversible. This fibroblast endogenous inhibitor does not interfere with the proliferation of DNA synthesis by human lymphocytes, bronchial carcinoma cells, or HeLa cells. The activity does not appear to be species specific. Therefore, we suggest that it is quite possible that the control of fibroblast proliferation resides in a fibroblast chalone. Diploid human fibroblasts, in contrast to chicken or mouse fibroblasts or heteroploid fibroblasts in general, stringently require serum for their proliferation. All of this mitogenic activity of calf serum can be concentrated in a molecular weight range around 100,000 daltons by ultrafiltration. All of the mitogenic activity within this molecular weight class can be concentrated at a pH of 5.2 via isoelectric focusing, and all of the activity at this isoelectric point can be concentrated in one peak on preparative polyacrylamide gel electrophoresis. This latter material is homogeneous at three different pH's in analytical gel electrophoresis as well as in SDS electrophoresis. This purified serum mitogen for diploid human fibroblasts in vitro also works in vivo and represents as much as 0.5% of calf serum protein, albeit there is much less of this protein in adult cow or horse. It is composed of two equal subunits weighing about 60,000 daltons each and contains about 2 moles of sialic acid, one S-S bond, and 6 moles of hexose per subunit. There is a reciprocal relationship between the biological activity of fibroblast inhibitor and serum mitogen, but there is no apparent direct interaction between these two proteins. Addition of pure serum mitogen to diploid human fibroblasts in vitro results in the release of commensurable chalone activity into the medium and a reciprocal loss of mitogen from the medium. Therefore, we propose that serum contains a single macromolecule which competes with endogenous chalone on the surface of diploid human fibroblasts and that this functions as an anti-chalone for the fibroblast.
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PMID:Circulating factors controlling cell proliferation. 13 64

After the administration of 3-H-testosterone to castrated hamsters, extracts from crude nuclei were separated into bound and free fractions by gel filtration of Sephadex G-25, Subsequent analysis by thin-layer chromatography and recrystallization showed that dihydrotestosterone was the predominant radioactive steroid in the bound fraction and that it increased steadily with time until 1 hr after the injection. Further purification of the nuclear fraction showed an abundance of dihydrotestosterone in the nuclei. The binding was significantly decreased by pronase treatment, only slightly affected by deoxyribonuclease, and remained unaffected by ribonuclease. From the elution pattern on Sephadex G-200, the molecular weight of the binding macromolecule was estimated to be 3 times 10-4 daltons.
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PMID:The intranuclear binding of 17 beta-hydroxy-5 alpha-androstan-3-one and testosterone by hamster sebaceous glands. 16 88

Prostaglandin E 9-ketoreductase was purified from chicken heart by ammonium sulfate fractionation, and DEAE-Sephadex, hydroxylapatite and phosphocellulose chromatography. Two peaks of activity were resolved during the phosphocellulose chromatographic step. Both peaks were stimulated by a substance that was not bound to the phosphocellulose column. This stimulatory substance was destroyed by treatment with phosphodiesterase and 0.1 M NaOH. It was heat-stable (100 degrees, 2 min), nondialyzable, and resistant to treatment with pronase, ribonuclease, and deoxyribonuclease; but it was dialyzable after heating or digestion with pronase. Sodium pyrophosphate also enhanced the activities of the prostaglandin E 9-ketoreductases as did angiotensin I; but not angiotensin II. In the presence of 3':5'-cyclic AMP, AMP, or several other ribonucleotides, the enhancing effects of the natural stimulatory substance, sodium pyrophosphate or angiotensin I were blocked, but these ribonucleotides themselves had little effect on the enzymes activity. The substrate specificities of the two prostaglandin E 9-ketoreductases were also studied. Both the 9-keto group and the 15-keto group of 15-ketoprostaglandin F2 alpha could be converted to the corresponding hydroxyl group; the 15-keto group was reduced faster than the 9-keto group. Prostaglandin D2, a prostaglandin with a 9-hydroxyl and an 11-keto group, could not be converted to prostaglandin F2 alpha nor could cyclohexanone be converted to cyclohexanol by the prostaglandin E 9-ketoreductase.
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PMID:Purification and regulatory properties of chicken heart prostaglandin E 9-ketoreductase. 16 95

Treatment of neuroblastoma cells with dibutyryl-adenosine 3':5'-monophosphate or adenine induced axon formation and a three-fold increase in the polyadenylate, poly(A), content of the polysomal mRNA. The extracted poly(A) contained 90% adenylic acid and showed a mobility of 6--7 S in dodecylsulfate-polyacrylamide gel electrophoresis. Treatment with dibutyryl-adenosine 3':5'-monophosphate or adenine, also induced a 4--6 fold increase in a nuclear enzymic activity that incorporated [3H]ATP to an acid-insoluble polymer in a cell-free system. This polymer, like poly(A) extracted from the polysomal mRNA, was bound at high salt concentration to nitrocellulose filters. [3H]ATP incorporation was Mg2+-dependent, sensitive to ribonuclease and EDTA and resistant to deoxyribonuclease and actinomycin D. There was no incorporation of [3H]UTP or [3H]dTTP and addition of TUP, CTP and GTP did not increase the incorporation of [3H]ATP. 5-Bromodeoxyuridine induced axon formation of neuroblastoma cells and poly(A) polymerase activity, without increasing the poly(A) content in the polysomal mRNA. The results indicate that induction of axon formation of neuroblastoma cells is associated with an increase in the activity of poly(A) polymerase. It is suggested that the induction of this enzyme may be generally involved in cell differentiation.
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PMID:Induction of polyadenylate polymerase and differentiation in neuroblastoma cells. 17 99

In Anacystis nidulans, upon infection with cyanophage AS-1, after a lag period of 1 h the level of deoxyribonuclease (DNase) activity increaded rapidly up to 15- to 20-fold in 4 to 5 h in the light. In contrast, the ribonuclease and phosphomonoesterase activities increased significantly only 4 to 5 h after infection, i.e. as late as 1 h prior to lysis. In complete darkness, the nuclease levels remained unaltered. However, when the infected cells were exposed to light for 1 or 2 h after infection, the DNase level increased essentially to the same extent in the dark as in continuous light, although the complete replication cycle of the virus was impaired in the dark and cells lysed only in the continuously illuminated cultures. Inhibition of photosystem II with 3-(3,4-dichlorophenyl)-1-dimethylurea during the early illumination period strongly decreased the subsequent, infection-dependent increase in DNase activity in the dark. The virus-induced increase in DNase activity was also inhibited by chloramphenicol. The data suggest that, in spite of the obligate photoautotrophic nature of A. nidulans, dark metabolism is able to support fully the formation of some specific proteins if the triggering of their synthesis takes place in light.
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PMID:Formation in the dark, of virus-induced deoxyribonuclease activity in Anacystis nidulans, an obligate photoautotroph. 17

The action of deoxyribonuclease, ribonuclease, perchloric acid, and pronase on the fine structure of basal bodies of sectioned Paramecium was observed as part of a more extensive autoradiographic electron microscope analysis directed toward the problem of basal body DNA. DNase was found to have no detectable effect on basal body fine structure. Pronase first solubilized the linkers and C tubules of the triplets, then attacked the protein portion of the axosome, a localized portion of the ciliary axoneme adjacent to the distal end of the basal body, the rim fiber, and newly described lumen spiral complex. Prolonged pronase treatment disrupted the remaining microtubular elements, basal body plates, and cartwheel. RNase removed material from the axosome and the lumen complex, a conspicuous structure occupying the central portion of the basal body and consisting of a twisted or looped 90-A diam fiber or, more probably, pair of fibers, in association with large, dense granules. The apparent removal of both RNA and protein from this basal body structure by either of the two corresponding enzymes suggests an unusual organization of the two components. Observations from this and other laboratories suggest that the basal body RNA is single stranded. Its function is unknown but alternatives are discussed.
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PMID:Effects of nuclease and protease digestion on the ultrastructure of Paramecium basal bodies. 17 69

Primary human amnion cell monolayers which had been treated with DEAE-dextran, washed, and then inoculated with sonicated cells of the EB3 line of Burkitt's lymphoma cells developed foci of transformed amnion cells 7 to 14 days later. When either the DEAE-dextran or the sonicate was omitted, no significant transformation was found. The foci consisted of enlarging mounds of rapidly dividing cells, which upon subculturing continued their high miotic activity; and strains or lines of the transformed amnion cells were thus readily established. The modal number of chromosomes in such lines was 65 instead of the normal 46. Not all human amnions yielded cells transformable by EB3 cell sonicate, as determined by direct comparisions using the same cultural conditions and testing with the same fresh sonicate preparation in the same experiment. Overall, it appeared that only about 40 to 50% of the amnions yielded transformable cell monolayers; the rest gave monolayers apprently completely refractory to the transformation. The transformed amnion cells contained nuclear and cytoplasmic Epstein-Barr virus (EBV) antigen(s), as revealed by indirect immunofluorescence tests. EB3 cell sonicate also caused the appearance of rapidly growing transformed cell foci on secondary rat embryo cell monolayers which had been sensitized with DEAE-dextran. Calcium in the cell maintenance medium decreased the number of transformed foci found, both on the human and on the rat cell monlayers. Sonicates of cultured normal human leucocytes had no such transforming activity for either the human or the rat cells. The transforming agent in EB3 cell sonicate was completely destructible by either deoxyribonuclease or trypsin, but not by ribonuclease, and was not neutralizable by anti-EBV serum. The simplest interpretation of these results is that the transforming agent is part of all of the EBV DNA plus some necessary protein, with both the DNA and the protein accessible to hydrolytic enzyme action.
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PMID:Use of a transfection method to demonstrate a monolayer cell transforming agent from the EB3 line of Burkitt's lymphoma cells. 18 Feb 48


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