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)

Nuclei were prepared by sucrose sedimentation of liver homogenates from rats given (125)I-labeled triiodothyronine in vivo. The nuclear extract obtained by treatment of the nuclear pellet with 0.4 M KCl contains the [(125)I]triiodothyronine that had been injected in vivo bound to protein(s). The triiodothyronine bound to nuclear protein(s) in vivo does not readily exchange with triiodothyronine added to the extract in vitro. This triiodothyronine.nuclear extract complex retains triiodothyronine during dialysis or exposure to anion exchange resin and migrates as a broad band on agarose-gel electrophoresis. It is rapidly destroyed by Pronase, by 8 M urea, and by p-chloromercuribenzoic acid, but not by RNase or by DNase. It is also susceptible to thermal inactivation at 37 degrees , possibly through changes in the affinity of triiodothyronine to the nuclear binding protein(s), since the bound triiodothyronine becomes more readily dialyzable, is absorbed by an anion exchange resin, but retains its characteristic mobility on electrophoresis. The triiodothyronine.nuclear extract complex formed in vivo binds to crude liver chromatin in vitro at low salt concentration, but can be completely extracted again at KCl concentrations greater than 0.2 M.
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PMID:Nuclear triiodothyronine-binding protein: partial characterization and binding to chromatin. 453 Feb 84

Brief exposure of Chinese hamster ovary cell monolayers prelabeled with [(32)P]phosphate and [(3)H]leucine to 1 mug/ml of trypsin under conditions in which cells remain fully viable causes the release of macromolecular (32)P and (3)H. Whereas ribonuclease treatment was found to affect markedly both the (32)P and (3)H radioactivity, Pronase treatment had little effect on the macromolecular (32)P. Treatment of cells prelabeled with [(3)H]glucosamine and [(32)P]phosphate with insolubilized papain also revealed a parallel release of macromolecular glucosamine together with ribonuclease-susceptible macromolecular phosphate. Lactoperoxidase-mediated radioiodination of surface components in cells prelabeled with [(32)P]phosphate revealed electrophoretic comigration between the (125)I and the (32)P that are removed from the cells by mild proteolysis. Growth of the cells in Bt(2)cAMP-testosterone altered the kinetics of release and nature of the macromolecular (32)P liberated by proteolysis.
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PMID:An "external" RNA removable from mammalian cells by mild proteolysis. 453 Oct 29

The vitamin B(12)-binding property of Lactobacillus leichmannii ATCC 7830 has been studied. The organism could bind 0.52 mug of B(12) per mg of cells. With regard to the cellular site for B(12) accumulation, three-quarters of the B(12) bound to the cell was found in the crude cell wall fraction, and the remaining one-quarter was found in the particulate (ribosome) fraction. After receiving enzymatic treatments with ribonuclease, lipase, and trypsin, the wall fraction retained three-fifths of the initial B(12). The possibility of cross-contamination of the wall and particulate fractions was excluded by measuring the contents of ribonucleic acid and hexosamines in each fraction. The B(12)-binding activity of the wall was destroyed by pretreatment of the wall with pepsin, Pronase, or trypsin. However, once bound to the wall, the B(12) was not released by the same treatments. These facts suggest that B(12) is bound to a polypeptide in the wall on which these enzymes act and that, once bound, B(12) somehow inhibits the enzymatic actions as described earlier with L. delbrueckii no. 1. A B(12)-polypeptide complex was isolated by treatment with 0.2 n HCl from walls to which B(12) had been bound. The complex was then purified. The complex moves as a single band on polyacrylamide gel electrophoresis. Its molecular weight was estimated around 21,500 with microheterogeneity on a Sephadex G-75 column. The mode of B(12) binding was found to be similar to that of L. delbrueckii.
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PMID:Further studies on the binding of vitamin B 12 to the cell wall of a B 12 -requiring Lactobacillus. 455 Jun 59

An electron microscopy study has been made of the effects of dissolution of the plasma membrane of Escherichia coli with sodium dodecyl sulfate (SDS) on the organization of the nucleoplasm and the cytoplasm. The alterations observed in time course experiments were related to absorbance changes and to release of macromolecules from the cells. As the cells became plasmolyzed, under the conditions used, the first visible effect of SDS was a collapse of the plasmolysis spaces. This was accompanied by a displacement of the nuclear material which then appeared in broad contact with the redeployed plasma membrane. This initial displacement of nuclear material to the cell border may indicate an association between the nucleoplasm and the plasma membrane. Upon further dissolution of the plasma membrane, the nuclear material receded from the cell margin and contracted into an axial filament. Meanwhile, the cytoplasm dissociated into an amorphous, Pronase-sensitive component and an electron-opaque, granular one sensitive to ribonuclease. The latter represented one continuous area of ribosomal structures surrounding the nucleoplasm, an organization which did not occur when the cells were inhibited with rifamycin before SDS treatment. During prolonged SDS interaction, approximately 65% of the cellular protein, 25% of the ribonucleic acid and 40% of the deoxyribonucleic acid were released from the cells concomitant with the disappearance of the amorphous cytoplasmic part, expansion of the ribosomal aggregate, and rearrangement of the nuclear material at the cell periphery. The observations support the contention that all ribosomal structures bear a direct relationship with the nucleoplasm.
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PMID:Effects of treatment with sodium dodecyl sulfate on the ultrastructure of Escherichia coli. 455 30

Host-free growth and reproduction of a host-dependent strain of Bdellovibrio bacteriovorus incubated with an extract from host cells were studied. The morphological changes occurring in the cells were correlated with deoxyribonucleic acid (DNA) synthesis as measured by labeled nucleotide or orthophosphate incorporation. The host-free developmental cycle of Bdellovibrio is similar to that of the two-membered system; the early loss of flagella, the elongation into filaments, and multiple fission into flagellated progeny are typical for both host-free and intraperiplasmic development of bdellovibrios. Filament length and time of division appear to depend on the concentration of the host extract. Host extract was found to be heat stable and DNase stable, and Pronase sensitive and RNase sensitive. Addition of ribonucleic acid to the extract medium at various times during the Bdellovibrio growth cycle demonstrated that host extract is required continuously during the cycle for growth. The observations reported give a unified picture of Bdellovibrio development and allow for the suggestion that wild-type bdellovibrios depend upon the presence of some host factor for induction of DNA synthesis, whereas depletion of host factor triggers division. The ecological implications of such host dependence are discussed.
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PMID:Growth cycle of predacious Bdellovibrios in a host-free extract system and some properties of the host extract. 458 8

Ribosomes of strain NOR-7 of group B Neisseria meningitidis were isolated by a procedure that included treatment of the cells with sodium dodecyl sulfate, disruption in a French pressure cell, and differential centrifugation. These preparations consisted of 66% ribonucleic acid and 24% protein and sedimented as a single component with a constant of approximately 66S. When used in immunodiffusion tests with homologous rabbit antiserum, untreated ribosomes formed two precipitin lines, when treated with ribonuclease three lines, and when Pronase-digested only one distinct line. Qualitatively indistinguishable reactions were obtained with the same antiserum and ribosomes from group A meningococci, but no precipitation occurred with those of Escherichia coli. When injected into mice, group B ribosomes elicited an increase in the number of antibody-producing spleen cells demonstrable by the hemolytic plaque technique using unsensitized sheep erythrocytes. Sensitization of the erythrocytes with increasing amounts of supernatant fluid of meningococcal cultures progressively reduced the number of demonstrable plaque-forming cells. Neuraminidase treatment of the erythrocytes increased immune hemolysis, whereas Pronase digestion reduced it. Injected mice were protected against homologous and heterologous meningococcal challenge. Both hemolysis and protection-inducing activities of the ribosomes were unimpaired by ribonuclease, but were reduced by Pronase. It is concluded that the immunological response elicited by the meningococcal ribosomes does not involve the group-specific carbohydrate antigen. The immunological mechanism by which the mice are protected against meningococcal challenge remains unknown.
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PMID:Response of mice to injection of ribosomal fraction from group B Neisseria meningitidis. 462 60

An auxotrophic strain of E. coli K12 treated with CaCl(2) was transformed for several markers at a frequency of up to 10(-6) per recipient cell by a DNA preparation isolated from a prototrophic strain. The transforming activity of the DNA preparation was eliminated by treatment with DNase, heat, or sonication, whereas RNase or Pronase treatment had little effect. Two closely linked genetic markers (leu and ara) showed a high degree of cotransformation linkage when high molecular weight DNA was used, but the linkage was almost completely eliminated when sheared, smaller molecular weight DNA was used. There is genetic evidence that the transformation is a result of the replacement of the preexisting genetic marker on the chromosome by that of the donor DNA.
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PMID:Genetic transformation in Escherichia coli K12. 463 Jun 12

Intracisternal A particles, known primarily for their association with various tumors, have been shown to contain high-molecular-weight (HMW) ribonucleic acid (RNA) by velocity centrifugation, using linear glycerol gradients. This HMW RNA is sensitive to ribonuclease digestion and alkali treatment but is resistant to Pronase treatment. By a double-labeling experiment, HMW RNA was shown to be intrinsic to intracisternal A particles and not to have resulted from cytoplasmic polysomal RNA aggregation. By a reconstitution experiment, it was determined that the results were not due to C-type virus contamination. The synthesis of HMW RNA in intracisternal A particles is inhibited by actinomycin D and ethidium bromide. These observations emphasize that there are probably some taxonomic relationships between intracisternal A particles and oncogenic RNA viruses.
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PMID:Analysis of high-molecular-weight ribonucleic acid associated with intracisternal A particles. 468 4

Newly synthesized (3)H-labelled DNA was extracted from baby hamster kidney cells (BHK-21/C13 cells) and was shown to possess single-stranded properties when examined by column chromatography on benzoylated naphthoylated DEAE-cellulose, hydroxyapatite and methylated albumin on kieselguhr, and by its affinity for nitrocellulose filters. Some of the newly synthesized DNA was shown to be of lower molecular weight than the bulk of the DNA when examined by alkaline sucrose-density-gradient centrifugation. The properties observed were not affected by treatment of the DNA with ribonuclease, Pronase or amylase. The effect of the size of the DNA on its observed properties was examined and is discussed. It is concluded that DNA synthesis in BHK-21/C13 cells proceeds according to the discontinuous-mechanism model in at least one of the strands.
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PMID:Synthesis of deoxyribonucleic acid in BHK-21-C13 cells. 473 96

Spermatozoa from the cauda of the epididymis of the hamster and rat were incubated with [5-(3)H]uridine and glucose. By using a procedure avoiding bacterial and other cellular contamination, sonic extracts were prepared and digested with deoxyribonuclease and Pronase. Radioactive RNA of high molecular weight was isolated by two methods: (a) gel filtration on Sephadex G-75 columns and (b) polyacrylamide-gel electrophoresis in which it migrated in the region of 28S and 23S RNA markers. The macromolecules were alkali-labile and hydrolysed by ribonuclease. From (3)H radioactivity and E(260) of the isolated RNA the rate of incorporation of uridine into RNA of spermatozoa was calculated to be 0.1-0.5nmol/h per mg of RNA.
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PMID:Ribonucleic acid synthesis by spermatozoa from the rat and hamster. 474 26


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