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)

Precursor mRNA (pre-mRNA) was extracted from erythroid enriched bone marrow cells of the rabbit by the methods of Georgiev and Mantieva modified by Markov and Arion and of Holmes and Bonner, respectively. Density gradient centrifugation, base analysis and the effects of alpha-amanitin and actinomycin D on the synthesis of the cellular RNA showed signs of degradation in the rRNA-free 85 degrees C-fraction of the preparation according to Georgiev and Mantieva and a substantial rRNA contamination of the 65 degrees C-fraction. This RNA-fraction as well as the total RNA-preparation extracted according to Holmes and Bonner was purified from rRNA by affinity chromatography on poly(U)-Sepharose. Poly(A)+-RNA of all size-classes, among it a substantial amount of high molecular weight RNA (greater than 45 S), was isolated by this purification procedure. Especially the extraction according to Holmes and Bonner yields high molecular weight material but the critical step of this procedure often resulting in degradation of the RNA is the DNase treatment of the heavily DNA-contaminated total RNA-preparation either due to RNase contamination of the DNase or to the existence of RNase in the less intensive deproteinized RNA. The investigated cellular system is characterized by a very intensive rRNA synthesis which is typical for cells in the early stages of hematopoiesis. In contrast to investigations with purified RNA-polymerases and subcellular systems, but in accordance with data of in vivo experiments, alpha-amanitin inhibits both the pre-mRNA and the pre-rRNA synthesis.
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PMID:Pre-mRNA from erythroid enriched bone marrow cells of the rabbit. II. Characterization of pre-mRNA isolated by phenol extraction and poly(U)-Sepharose chromatography. 74 68

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

The mixing of two histoincompatible human lymphocyte cell lines generated the release of a soluble factor which was capable on non-specifically enhancing the in vitro immune response of normal mouse spleen cells against sheep erythrocytes. The mediator was secreted into the supernatant of the allogeneic cell cultures within 24 h of cultuvation. The human enhancing factor (HEF) must be added to assay cultures on day 2, of a 5-day culture period, for its activity to be manifest. HEF was resistant to DNase, RNase and heating at 56 degrees for 30 min, but was inactivated by exposure to protease or elevated temperature (80 degrees for 30 min). The molecular weight of HEF, purified by ammonium sulphate fractionation, followed by Sephadex gel filtration, DEAE-cellulose chromatography and SDS-polyacrylamide gel electrophoresis, was approximately 38,000 Daltons.
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PMID:Partial characterization of an immunoenhancing factor from allogeneic human lymphocyte cell lines. 76 66

Nerve growth factor (NGF) receptor binding in membrane fractions of rabbit superior cervical ganglia has been measured after treatment with a variety of enzymes, protein-modifying reagents, and ions. Receptor binding is degraded by low concentrations of trypsin but is much less sensitive to alpha-chymotrypsin. Low concentrations of phospholipase A from Vipera russelli decrease NGF receptor binding by lowering the number of binding sites, while phospholipase A preparations from Crotalus terrificus terrificus and bee venom do not affect binding. Phospholipase C and D, neuraminidase, DNase, and RNase have minimal effects on receptor binding. NGF receptor binding appears to be absolutely dependent upon calcium ion. Removal of calcium from the incubation medium greatly reduces binding as does treatment with EDTA. Maximal receptor binding occurs at 5 mM calcium. Magnesium and sodium are unable to substitute for calcium. Receptor binding is greatly reduced by treating membranes with 2-hydroxy-5-nitrobenzyl bromide, 2-methoxy-5-nitrobenzyl bromide, diazonium tetrazole, and tetranitromethane. NGF receptor sites can be protected from 2-hydroxy-5-nitrobenzyl bromide by incubation with NGF.
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PMID:Nerve growth factor receptor binding. Influence of enzymes, ions, and protein reagents. 80 4

An increase in total RNase activity was associated with three patterns of cell senescence in corn (Zea mays L.) (cv. WF9 X 38-11) cob parenchyma during the first two weeks following silking, stalk pith tissue after internode elongation and the first developed leaf of seedlings. Stalk pith tissue had two RNase activities, one inhibited by EDTA and one not. Both remained in approximately equal amounts in young to old pith tissue. In the first developed leaf of seedlings, the activity not inhibited by EDTA remained at a constant low level during the period studied, while the other activity varied. No inhibition by EDTA was found in cob parenchyma tissue. Incubation of sections of cob parenchyma and stalk pith tissues suggested that the total RNase activity of cob parenchyma is very stable and that of stalk pith tissue is relatively stable. An age-related increase in DNase activity was found in stalk pith tissue and in the first developed leaf of seedlings, but not in cob parenchyma tissue.
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PMID:Relationship of nuclease activity and synthesis to senescence of corn (Zea mays L.) stalk pith, cob parenchyma and first developed leaf tissues. 82 86

An ovarian cystadenocarcinoma-associated antigen (OCAA) was found to be common to all serous and mucinous cystadenocarcinomas of the ovary. It was apparently absent in tissues of normal reproductive organs. Furthermore, OCAA was not detected in benign ovarian serous and mucinous cyst-adenomas or in any other gynecologic or nongynecologic cancers thus far tested. The antigenic determinant of OCAA was immunologically unrelated to the carcinoembryonic antigen, other known tumor antigens, or the histocompatibility antigens. We purified and partially characterized OCAA. The antigen was a high-molecular-weight glycoprotein soluble in 0.6 M perchloric acid. It consisted of about 50-60% protein (based on dry wt). Amino acid composition in OCAA was characterized by a high percentage of threonine, serine, proline, and valine. Galactose and N-acetylglucosamine were the principal carbohydrate constituents. The antigenic activity was resistant to treatment with trypsin and protease and also to treatment with DNase, RNase, and N-acetylneuraminidase. The antigenicity was considerably reduced by mild periodate oxidation.
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PMID:Tumor-associated antigen for cystadenocarcinomas of the ovary. 82 81

The antitumor effect of reserve polysaccharide, paramylon, from Euglena gracilis on the transplantable sarcoma-180 was examined in mice. This polysaccharide had an effect similar to that of lentinan. Paramylon, in a dose of 1 mug/g body weight, injected intraperitoneally 24 hr after tumor implantation had an inhibitory effect on the tumor growth, although without causing complete regression of the tumor. Alkaline-treated paramylon had a similar effect but at a smaller concentration than the native one. The inhibitory activity was not lost when the paramylon preparation was treated with pronase, DNase, or RNase. The antitumor effect might be a lymphocyte-mediated process. In tumors that were regressing after treatment, there was extensive outpouring of lymphoid cells with plasma cells and macrophages. A test conducted using paramylon ruled out the possibility of an interferon-mediated inhibiotry effect on tumor growth.
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PMID:Antitumor activity of paramylon on sarcoma-180 in mice. 82 42

A fraction containing membrane-bound tobacco mosaic virus RNA replicase was isolated form tobacco mosaic virus-infected tobacco callus cultures. The replicase activity reached a maximum 60 h after inoculation and then declined. The enzyme activity was insensitive to actinomycin D and DNase. The corresponding fraction from healthy callus contained essentially no activity. The viral RNA synthesis in vitro proceeded linearly for 30 min and required the four nucleotide triphosphates and Mg2+ ions. Mn2+ was a poor substitute for Mg2+. During RNA synthesis the product was at least 70% resistant to RNase in 2X SSC (0.15 M NaCl plus 0.015 M sodium citrate), but completely digested by RNase in 0.1X SSC. Analysis of the product by polns) that appeared to be replicative form and a partially RNase-resistant structure similar to replicative intermediate form. Washing the membrane-bound replicase with Mg2+-deficient buffer solubilized enzyme. The solubulized enzyme was further purified by DEAE-Sephadex column chromatography. The DEAE-purified enzyme was nearly completely dependent upon tobacco mosaic virus RNA for activity. Analysis of the product on a sucrose gradient revealed a double-stranded RNA with sedimentation of 16S and smaller heterogeneous RNase-sensitive products.
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PMID:In vitro replication of tobacco mosaic virus RNA in tobacco callus cultures: solubilization of membrane-bound replicase and partial purification. 83 35

Sucrose density gradient fractionation of isolated rat liver mitochondrial DNA ordinarily yields two peaks, one at 39 S, the other at 27 S. However, when these mitochondria are first incubated with a labeled DNA precursor, a labeled peak at about 8 S is also observed. Is this low molecular weight 8 S DNA merely an artifact of contamination or breakdown, or is it a functioning part of the mitochondrial genome? That it is not a nuclear contaminant is shown by: (a) the absence of nuclei or nuclear fragments in active mitochondrial preparations; (b) the insensitivity of 8 S DNA synthesis to treatment of mitochondria with DNase and RNase; (c) the ability of inner membrane preparations to synthesize this DNA; (d) the ability of atractyloside to inhibit incorporation of [3H]dATP into 8 S and 39 S or 27 S DNA equally; (e) the labeling of 8 S DNA (as well as 39 S and 27 S DNA) but not of nuclear DNA after the administration in vivo of [3H]thymidine. The evidence that 8 S DNA is not an artifact resulting from DNA breakdown during mitochondrial incubation or DNA isolation is as follows: (a) 8 S DNA can be isolated from unincubated mitochondrial; (b) 8 S DNA becomes labeled when labeled DNA precursors are administered in vivo; (c) 8 S DNA biosynthesis continues in the complete absence of labeled 39 S or 27 S DNA (whose synthesis is repressed by ethidium bromide), making it unlikely that 8 S DNA is formed from the breakdown of 39 S or 27 S DNA; (d) substitution of milder methods of DNA extraction does not decrease 8 S DNA labeling; moreover, the usual conditions of extraction, when applied to purified 39 S and 27 S DNA, do not generate 8 S DNA, nor does an additional mitochondrial washing cycle; (e) the specific radioactivity of 8 S DNA is higher than that of 39 S or 27 S DNA, making it improbable that the latter forms are precursors of 8 S DNA. Since 8 S DNA is double-stranded, it is not identical to the 7 S fragment of D loop DNA. The hypothesis that the artifactual nicking of those DNA molecules which contain opposing D loops leads to the release of double-stranded fragments was tested. The DNA which was released was predominantly (and probably completely) single-stranded. We conclude that 8 S DNA is probably not an artifact and studies are in progress on its function.
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PMID:Biosynthesis of mitochondrial DNA. Is 8 S DNA an artifact? 85 9

Severe degradation of high molecular weight RNA was shown to occur during incubation with commercially purified DNase. Most of the RNase activity could be removed by passage of the DNase through a column of agarose-coupled amino phenylphosphoryl-uridine-2' (3')-phosphate. Incubation with the treated DNase caused only minimal alteration of the sedimentation pattern of high molecular weight nuclear RNA, determined under partially denturing conditions. No impairment of DNase activity was detected.
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PMID:Removal of RNase activity from DNase by affinity chromatography on agarose coupled aminophenylphosphoryl-uridine-2' (3')-phosphate. 86 76


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