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)

A soluble somatostatin-binding protein was detected in the cytosol fractions of various rat, human and bovine tissues. Maximum binding occurred at pH8.0-8.5 and was Ca(2+)-dependent. The specific binding of somatostatin per 10mug of cytosol protein from 12 rat tissues ranged between 36 and 15%, and 3% for peripheral blood cells. There was also substantial binding in cytosol from human anterior pituitary and liver, and bovine anterior pituitary. The specific binding in rat and human plasma in the presence of EDTA was only 1%. Gel filtration suggested a molecular weight of approx. 80000 for the somatostatin-binding protein from several sources. Exposure of the binding protein to trypsin eliminates somatostatin-binding activity but ribonuclease and deoxyribonuclease have no effect. The binding protein is thermolabile, ethanol-precipitable, and not completely specific for somatostatin. Bound (125)I-labelled [Tyr(1)]somatostatin is not easily displaced by excess of unlabelled somatostatin. The effects of dithiothreitol and mercaptoethanol on the binding of (125)I-labelled [Tyr(1)]somatostatin to the binding protein suggests that binding involves two sequential steps, first loose binding, then disulphide linkage. Since semipurified somatostatin-binding protein causes a dose-related inhibition of the binding of (125)I-labelled [Tyr(1)]somatostatin in radioimmunoassays for somatostatin, estimates of somatostatin content of tissue extracts by radioimmunoassay in some cases may be spuriously high. It is not yet clear whether the binding protein is a true cytosol protein or an easily solubilized membrane protein.
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PMID:Properties of soluble somatostatin-binding protein. 2 54

The peripheral membrane protein fraction released by washing Acholeplasma laidlawii membranes with low-ionic strength buffers contained about 50% of the total membrane-bound ribonuclease and deoxyribonuclease activities. The ATPase, NADH oxidase and p-nitrophenylphosphatase activities remained bound to the membrane even when EDTA was added to the wash fluids, and thus appear to belong to the integral membrane protein group. Serving as a marker for peripheral membrane proteins, the membrane-bound ribonuclease activity was solubilized by bile salts much more effectively than the integral membrane-bound enzymes. On the other hand, the solubilized ribonuclease showed a much lower capacity to reaggregate with other solubilized membrane components to membranous structures. Yet, most of the ribonuclease molecules which were bound to the reaggregated membranes could not be released by low-ionic strength buffer. The reaggregated membranes differed from the native membranes in the absence of particles on their fracture faces obtained by freeze cleaving, and by their much higher labeling by the [125-I]lactoperoxidase iodination system. These results suggest that most of the proteins are exposed on the reaggregated membrane surfaces, with very little, if any, protein embedded in its lipid bilayer core. Enzyme disposition in the A. laidlawii membrane was studied by comparing the activity of isolated membranes with that of membranes of intact cells after treatment with pronase or with an antiserum to membranes. The data indicate the asymmetrical disposition of these activities, the ATPase and NADH oxidase being localized on the inner membrane surface, while the nucleases are exposed on the external membrane surface.
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PMID:Characterization of the mycoplasma membrane proteins. V. Release and localization of membrane-bound enzymes in Acholeplasma laidlawii. 23 52

Moloney leukemia virus activated both the classical and alternative pathways of human complement. About 500,000 virions were required to detect activation of the classical pathway whereas 5,000 times as many virions were necessary to initiate the alternative pathway, indicating that in this system only the former is of biological significance. Disruption of the virus with Triton X-100 destroyed its ability to initiate the alternative pathway without affecting its ability to activate the classical pathway. After ultracentrifugation of disrupted virus the active component could be recovered in the supernate and was isolated by isoelectric focusing in granulated gels. Sodium dodecyl sulfate-polyacrylamide gel electrophoretic and analysis and cyanogen bromide digestion studies revealed that the activity resided in a methionine-containing protein having a pI of 7.5 and a molecular weight of approximately equal to 15,000 daltons. The purified protein interacts strongly with Clq and efficiently activates Cl. RNase and lipolytic enzymes had no effect on the isolated protein but incubation with trypsin resulted in loss of activity. Enzymatic digestion studies of surface-labeled virus indicate that the active protein is a viral membrane protein. On the basis of these results it is concluded that the complement receptor of Moloney leukemia virus is the surface protein p15E.
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PMID:Lysis of oncornaviruses by human serum. Isolation of the viral complement (C1) receptor and identification as p15E. 63 50

The incorporation of radiolabeled GTP into RNA in host-free Chlamydia trachomatis serovar L2 organisms was investigated. The incorporation was partially inhibited by rifampin and dactinomycin and hydrolyzed by RNase. RNA made by host-free chlamydiae consisted mainly of species of fewer than 800 bases in size, although 16S and 23S species were noted by agarose-gel electrophoresis. The hybridization of radiolabeled host-free RNA to restriction fragments of the gene encoding the major outer membrane protein was analyzed; all regions of the gene were transcribed. The relative intensity of hybridization of host-free RNA made by chlamydiae isolated during the middle and late stages of the developmental cycle to the DNA of clones encoding gene products known to be made at these times in vivo indicated that the temporal patterns of host-free and in vivo transcription were similar. Radiolabeled RNA from 1- and 24-h host-free Chlamydia psittaci 6BC organisms hybridized to many of the same EcoRI and BamHI restriction fragments of C. psittaci genomic DNA, although some differences could be noted. When these RNAs were used to screen a partial C. psittaci genomic library in lambda gt11, plaques were identified that reacted mainly either with 1-h RNA or with 24-h RNA. Because RNA synthesized by host-free chlamydiae appears to be developmental cycle stage specific, transcripts made by host-free chlamydiae may be convenient probes that can be used to clone developmental stage-specific chlamydial genes.
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PMID:Developmental cycle-specific host-free RNA synthesis in Chlamydia spp. 169 76

Using cDNA cloning, ribonuclease protection, and Northern hybridization analysis, we showed that insulin gene expression occurs in yolk sac-derived fetal extraplacental membranes throughout the last half of rat fetal development. The mRNA product of the ancestral rat insulin II but not the duplicated rat insulin I gene was present in high copy number, and its abundance was regulated during development. Insulin mRNA was present in extraplacental membranes before pancreatic differentiation; membrane insulin mRNA content greatly exceeded that in pancreas until the last 2 days of gestation when content in each tissue became similar. Polyadenylation and intron splicing occurred at the same sites used in pancreas, but initiation of transcription occurred at multiple sites in membranes. Minces of membranes maintained in culture produced approximately 10 ng of radioimmunoassayable insulin/mg membrane protein/day. Over a 4-day period, approximately 50 times more insulin accumulated in medium than that present in membranes at the time of isolation. These studies indicate that yolk sac is a source for insulin during fetal development and that the mechanisms regulating insulin gene expression in this tissue differ from those in pancreatic beta cells.
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PMID:Rat insulin II gene expression by extraplacental membranes. A non-pancreatic source for fetal insulin. 265 99

The postsynaptic membrane of vertebrate neuromuscular synapses is enriched in the four subunits of the acetylcholine receptor (AChR) and in a peripheral membrane protein of Mr = 43 x 10(3) (43K). Although AChRs are virtually restricted to the postsynaptic membrane of innervated adult muscle, developing and denervated adult muscle contain AChRs at nonsynaptic regions. These nonsynaptic AChRs accumulate because the level of mRNA encoding AChR subunits increases in response to a loss of muscle cell electrical activity. We have determined the level of mRNA encoding the 43K subsynaptic protein in developing muscle and in innervated and denervated adult muscle. We isolated a cDNA that encodes the entire protein-coding region of the 43K subsynaptic protein from Torpedo electric organ and used this cDNA to isolate a cDNA that encodes the 43K subsynaptic protein from Xenopus laevis. We used the Xenopus cDNA to measure the level of transcript encoding the 43K protein in embryonic muscle and in innervated and denervated adult muscle by RNase protection. The level of transcript encoding the 43K protein is low in innervated adult muscle and increases 25- to 30-fold after denervation. The level of transcript encoding the alpha subunit of the AChR increases to a similar extent after denervation. Moreover, during development, transcripts encoding the 43K protein and the alpha subunit are expressed initially at late gastrula and are present in similar quantities in embryonic muscle. These results demonstrate that transcripts encoding the 43K protein and AChR subunits appear coordinately during embryonic development and that the level of mRNA encoding the 43K protein is regulated by denervation.
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PMID:Regulation of transcript encoding the 43K subsynaptic protein during development and after denervation. 307 52

The gene for ribonuclease T1 from Aspergillus oryzae has been chemically synthesized using the segmental support technique. An Escherichia coli clone producing the ribonuclease at high levels was constructed by linking the gene downstream to the region coding for the signal peptide of the OmpA protein (a major outer membrane protein of E. coli), using the secretion cloning vector pIN-III-ompA2. This strategy was employed in order to circumvent a possible toxic effect of the gene product on the host cell. Active ribonuclease containing four additional amino acids at the N-terminus could be isolated from the periplasmic fraction of the host. The final yield after purification was 20 mg enzyme/l liquid culture. With respect to immunological, catalytic and specific behaviour, no qualitative differences could be detected between the enzyme from the over-producing E. coli strain and ribonuclease T1 isolated from A. oryzae.
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PMID:Expression of the chemically synthesized gene for ribonuclease T1 in Escherichia coli using a secretion cloning vector. 313 Nov 42

A selective extraction procedure was developed for sequentially extracting a fraction containing the primary dehydrogenase and a fraction containing the cytochromes of the nicotinamide adenine dinucleotide (reduced form) (NADH) oxidase of Bacillus megaterium KM membranes. The primary dehydrogenase (NADH-2,6-dichlorophenolindophenol oxidoreductase) activity was extracted from sonically treated membranes with 0.4% sodium deoxycholate for 30 min at 4 C. The insoluble residue was extracted with 0.4% sodium deoxycholate in 1 m KCl for 30 min at 25 C. A combination of the two extracts and dilution in Mg(2+) gave good recovery of the original membrane NADH oxidase activity. The primary dehydrogenase fraction contained 41% of the membrane protein, no cytochromes, flavine adenine dinucleotide as the sole acid-extractable flavine, and most of the membrane ribonucleic acid (RNA). The cytochrome-containing fraction had 16% of the membrane protein, 61% of the membrane cytochrome with the same relative amounts of cytochromes a and b as the original membrane, no acid-extractable flavine, little RNA, and no oxidoreductase activity. The oxidoreductase fraction remained soluble after removal of deoxycholate whereas the cytochrome fraction became insoluble after removal of deoxycholate-KCl, but the precipitated fraction could be redissolved in 0.4% sodium deoxycholate. Treatment of both fractions with ribonuclease to destroy all of the RNA present did not affect the ability of the fractions to recombine into a functional oxidase unit. Treatment of either fraction with phospholipase A prevented restoration of a functional oxidase when the oxidoreductase and cytochrome fractions were treated in solution, but no affect on restoration of oxidase was observed when the phospholipase A treatment was carried out with the soluble oxidoreductase fraction and the insoluble cytochrome fraction.
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PMID:Separation of the primary dehydrogenase from the cytochromes of the nicotinamide adenine dinucleotide (reduced form) oxidase of Bacillus megaterium. 433 82

The amount of chloroplast ribosomal RNAs of Chlamydomonas reinhardtii which sediment at 15,000 g is increased when cells are treated with chloramphenicol. Preparations of chloroplast membranes from chloramphenicol-treated cells contain more chloroplast ribosomal RNAs than preparations from untreated cells. The membranes from treated cells also contain more ribosome-like particles, some of which appear in polysome-like arrangements. About 50% of chloroplast ribosomes are released from membranes in vitro as subunits by 1 mM puromycin in 500 mM KCl. A portion of chloroplast ribosomal subunits is released by 500 mM KCl alone, a portion by 1 mM puromycin alone, and a portion by 1 mM puromycin in 500 mM KCl. Ribosomes are not released from isolated membranes by treatment with ribonuclease. Membranes in chloroplasts of chloramphenicol-treated cells show many ribosomes associated with membranes, some of which are present in polysome-like arrangements. This type of organization is less frequent in chloroplasts of untreated cells. Streptogramin, an inhibitor of initiation, prevents chloramphenicol from acting to permit isolation of membrane-bound ribosomes. Membrane-bound chloroplast ribosomes are probably a normal component of actively growing cells. The ability to isolate membrane-bound ribosomes from chloramphenicol-treated cells is probably due to chloramphenicol-prevented completion of nascent chains during harvesting of cells. Since chloroplasts synthesize some of their membrane proteins, and a portion of chloroplast ribosomes is bound to chloroplast membranes through nascent protein chains, it is suggested that the membrane-bound ribosomes are synthesizing membrane protein.
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PMID:Ribosomes bound to chloroplast membranes in Chlamydomonas reinhardtii. 480 47

From Salmonella typhimurium LT2 hemA (delta-aminolevulinic acid requiring) 15 mutants were isolated which grew on the hydrophobic compound hemin. All had increased sensitivity to antibiotics such as vancomycin, bacitracin, novobiocin, erythromycin, rifampin, and oleandomycin, and were considered to be envelope mutants (Env-). Half the mutants were rough , based on altered bacteriophage sensitivity and deoxycholate sensitivity, whereas the remainder were smooth; three of the smooth mutants were studied in detail. They gave increased uptake of gentian violet but no increase in leakage of a periplasmic protein, RNase I. The total membranes and fractions from sucrose gradient centrifugations representing inner and outer membranes of the wild type and three mutants were examined by sodium dodecyl sulfate - polyacrylamide gel electrophoresis (SDS-PAGE) and isoelectric focussing - PAGE (IEF-PAGE). The major outer membrane proteins (molecular weights (MW)33 000, 34 000, 35 000, and 36 000) showed no or very little alterations in the Env- mutants. In SA1926 (env-52) one protein spot at MW 48 000, proven to be an outer membrane protein, was missing, whereas a new spot appeared nearby, and other proteins in this area of the gel were reduced. An Env+ transductant selected from this strain had the wild-type protein pattern restored. The two other Env- mutants had similar but not identical changes in protein composition.
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PMID:Isolation and characterization of hemin-permeable, envelope-defective mutants of Salmonella typhimurium. 701 21


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