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

---

Query: EC:3.1.26.9 (ribonuclease)
6,589 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A ribonuclease (RNAase) was isolated and purified from the urine of a 45-year-old man by column chromatographies on DEAE-Sepharose CL-6B, cellulose phosphate and CM-cellulose followed by gel filtrations on Bio-Gel P-100 and Sephadex G-75, and finally to a homogeneous state by SDS-polyacrylamide gel electrophoresis. The enzyme was designated RNAase 1. It was possible to detect RNAase 1 isozymes in urine and serum without difficulty using isoelectric focusing electrophoresis followed by immunoblotting with a rabbit antibody specific to RNAase 1. The existence of genetic polymorphism of RNAase 1 was detected in human serum utilizing this technique (Yasuda, T. et al. (1988) Am. J. Hum. Genet., in press). RNAase 1 in serum and urine seemed to exist in multiple forms with regard to molecular weight and pI value. Genetically polymorphic RNAase 1 was a glycoprotein, containing three mannose, one fucose, four glucosamine and no sialic acid residues per molecule, with a molecular weight of 16,000 and 17,500 determined by gel filtration and SDS-polyacrylamide gel electrophoresis, respectively. The enzyme was most active at pH 7.0 on yeast RNA substrate and inhibited remarkably by Cu2+, Hg2+ and Zn2+. It also showed definite substrate preference for poly(C) and poly(U), but much less activity against poly(A) and poly(G). Thus, the enzyme is a pyrimidine-specific RNAase.
...
PMID:Purification and characterization of a human urine ribonuclease (RNAase 1) showing genetic polymorphism. 336 53

The brain ribonucleases of rabbit, guinea pig, rat, mouse and gerbil were investigated by histochemical and biochemical methods. For the localization, the ribonucleases were electrophoretically transferred from cryostat sections to polyacrylamide gels. Elevated ribonuclease activities were found in the cortex, the basal ganglia, the hippocampal formation and the ventricles, whereas the corpus callosum and the internal capsule exhibited lower activities. The total RNA degrading activities of the brain extracts of the different species varied in a wide range. However, a pre-requisite for the measurement of acid soluble degradation products in the test system was the inactivation of endogeneous ribonuclease inhibitors, present in all extracts. Molecular weight analysis by means of SDS-polyacrylamide gel electrophoresis revealed a characteristic set of ribonucleases for each species, consisting of enzymes with different pH-optima.
...
PMID:Comparison of brain ribonucleases of rabbit, guinea pig, rat, mouse and gerbil. 336 57

A ribonuclease was isolated and purified to homogeneity from cobra venom. The enzyme was found to be homogeneous on SDS and non-SDS polyacrylamide gel electrophoreses, and high performance liquid chromatography. The purified enzyme hydrolysed poly(rC), but not poly(rA), poly(rU), poly(rG), poly(rI), or poly(rI).poly(rC). The presence of magnesium was found to be an essential requirement for the nucleolytic activity of this enzyme.
...
PMID:A new ribonuclease from cobra venom (Naja naja) showing specificity towards cytidylic acid. 359 67

An intracellular effect of nickel(II) which may be involved in its carcinogenic action is the alteration of normal DNA-protein binding. This effect of ionic nickel was studied in Chinese hamster ovary cells using several chromatin isolation methods in combination with SDS-polyacrylamide gel electrophoresis. DNA from cells incubated with (35S)-methionine or (35S)-cysteine to radiolabel protein was prepared by three methods: (solation of nuclei or nucleoids followed by chloroform-isoamyl alcohol (24:1 v/v) extraction and in some cases an additional extraction in the absence or presence of 2M NaCl, 40 mM EDTA or SDS; by isopycnic centrifugation through Cs2SO4 gradients containing 0.8% sarkosyl, 2.2 MCs2SO4, 1 mM NaCl and 10 mM EDTA; or by chromatin disaggregation and denaturation using 9 M urea, 2% 2-mercaptoethanol, 4% Nonidet P-40 +/- 2 M NaCl. DNA from nickel-treated cells consistently had more (35S)-methionine radioactivity associated with it than did DNA from untreated cells. This radioactivity was resistant to ribonuclease but sensitive to protease. Differential extraction using denaturing agents and high ionic strength followed by SDS-polyacrylamide gel electrophoresis revealed that most of the tightly bound proteins were nonhistone chromosomal proteins, and possibly histone 1. The enhancement of DNA-protein binding from nickel-treated cells was disrupted by SDS, suggesting that nickel ions do not function as classical bifunctional crosslinking agents. Since regulation of DNA replication and gene expression is dependent upon DNA-protein interactions, the effect of nickel in altering the extent of DNA-protein binding may interfere with this regulation and may contribute to the carcinogenic activity of nickel compounds.
...
PMID:Effects of nickel(II) on nuclear protein binding to DNA in intact mammalian cells. 362 Nov 37

A protein was isolated from plasma of partially (70%) hepatectomized rats that, injected in mice, increases the uptake of [3H]thymidine by liver DNA by 200-300% over that by injected control saline. The purification procedure consists essentially of three chromatography steps, employing Sephadex G-75, DEAE-cellulose and hydroxyapatite. The hepatic promoter (HP) preparation shows a single band in SDS/polyacrylamide (15%)-gel electrophoresis (silver stained), with an Mr of 64 000; its activity is suppressed by trypsin or pepsin and is unaffected by deoxyribonuclease or ribonuclease. On injection into mice (150 ng/mouse), it increases the mitotic index of the liver. It shows organ-specificity, acting on liver but not on spleen, kidney, lung or brain. In primary liver cultures, it produces an increase in uptake of [3H]thymidine into DNA in the range 1-10 ng/ml. In this system in vitro, it increases the uptake of 22Na+ immediately after addition.
...
PMID:Purification of a liver DNA-synthesis promoter from plasma of partially hepatectomized rats. 374 89

The majority of the protein mass of HeLa 40S heterogeneous nuclear ribonucleoprotein monoparticles is composed of multiple copies of six proteins that resolve in SDS gels as three groups of doublet bands (A1, A2; B1, B2; and C1, C2) (Beyer, A. L., M. E. Christensen, B. W. Walker, and W. M. LeStourgeon. 1977. Cell. 11: 127-138). We report here that when 40S monoparticles are exposed briefly to ribonuclease, proteins A1, C1, and C2 are solubilized coincidentally with the loss of most premessenger RNA sequences. The remaining proteins exist as tetramers of (A2)3(B1) or pentamers of (A2)3(B1)(B2). The tetramers may reassociate in highly specific ways to form either of two different structures. In 0.1 M salt approximately 12 tetramers (derived from three or four monoparticles) reassemble to form highly regular structures, which may possess dodecahedral symmetry. These structures sediment at 43S, are 20-22 nm in width, and have a mass near 2.3 million. These structures possess 450-500 bases of slowly labeled RNA, which migrates in gels as fragments 200-220 bases in length. In 9 mM salt the tetramers reassociate to form 2.0 M salt-insoluble helical filaments of indeterminant length with a pitch near 60 nm and diameter near 18 nm. If 40S monoparticles are treated briefly with nuclease-free proteases, the same proteins solubilized by nuclease (A1, C1, and C2) are preferentially cleaved. This protein cleavage is associated with the dissociation of most of the heterogeneous nuclear RNA. Proteins A2 and B1 again reassemble to form uniform, globular particles, but these sediment slightly slower than intact monoparticles. These findings indicate that proteins A1, C1, and C2 and most of the premessenger sequences occupy a peripheral position in intact monoparticles and that their homotypic and heterotypic associations are dependent on protein-RNA interactions. Protein cross-linking studies demonstrate that trimers of A1, A2, and C1 exist as the most easily stabilized homotypic association in 40S particles. This supports the 3:1 ratio (via densitometry) of the A and C proteins to the B proteins and indicates that 40S monoparticles are composed of three or four repeating units, each containing 3(A1),3(A2),1(B1),1(B2),3(C1), and 1(C2).
...
PMID:General organization of protein in HeLa 40S nuclear ribonucleoprotein particles. 398 2

A cytosolic factor that stimulates transcription in isolated nuclei was purified approximately 4000-fold to near homogeneity from rat liver. The molecular weight of the factor was determined as 47 000 by SDS-polyacrylamide gel electrophoresis. The factor had no detectable deoxyribonuclease and protease activity but showed ribonuclease inhibitor activity. The factor could stimulate transcription in isolated nuclei by 50% at about 3.0 ng and the maximal stimulation was about 100%. When [gamma-S]ATP and [gamma-S]GTP were included in the reaction, the factor stimulated the synthesis of RNA which was able to bind to a mercury-Sepharose column and about 80% of the bound RNA was sensitive to a low concentration of alpha-amanitin. When heparin was added before initiation to preincubation mixture containing RNA polymerases II and DNA, a small but definite incorporation of [14C]UTP was observed. The factor alone had no stimulatory effect on the heparin-resistant incorporation of [14C]UTP but, in the presence of two rat liver nuclear fractions, phosphocellulose 0.5 and 1 M KCl step fractions, could stimulate the incorporation above the level with the combination of the two nuclear fractions. Antibody raised against the factor inhibited accurate transcription from the adenovirus 2 major late promoter in a nuclear lysate from Ehrlich ascites tumor cells, and the inhibition was neutralized by the factor.
...
PMID:Purification of a cytosolic factor from rat liver that stimulates transcription in isolated nuclei and its action on purified RNA polymerase II-DNA system. 407 43

Two ribonuclease activities have been isolated from macrophage culture medium. SDS-electrophoresis gave a molecular weight of 26,000 for both RNAases. The two RNAases differ only slightly in their enzymic properties. They are optimally active at neutral and slightly alkaline pH, and are not activated by monovalent or divalent cations or by spermine. Cu(II), Zn(II), Mn(II) and heparine inactivate them but they are not affected by the RNAase inhibitor from rat liver. They both degrade RNA endonucleolytically to mono- and oligonucleotides. They react to synthetic polynucleotides, especially poly(C), but do not degrade the synthetic double-stranded RNA poly(I) . poly(C), or double or single-stranded DNA. RNAase 1 inhibits DNA synthesis and increases degradation of RNA in granulation-tissue fibroblasts but RNAase 2 at the same concentration does not have these effects.
...
PMID:Purification of two ribonucleases from macrophage culture medium and studies on their effect on granulation-tissue fibroblasts. 616 35

We have examined the secretogogue responsiveness and the pattern of secretory proteins produced by a transplantable rat pancreatic acinar cell tumor. Dispersed tumor cells were found to discharge secretory proteins in vitro when incubated with hormones that act on four different classes of receptors: carbamylcholine, caerulein, secretin-vasoactive intestinal peptide, and bombesin. With all hormones tested, maximal discharge from tumor cells was only about one-half that of control pancreatic lobules, but occurred at the same dose optima except for secretin, whose dose optimum was 10-fold higher. Biochemical analysis of secretory proteins discharged by the tumor cells was carried out by crossed immunoelectrophoresis and by two-dimensional isoelectric focusing-SDS polyacrylamide gel electrophoresis. To establish a baseline for comparison, secretory proteins from normal rat pancreas were identified according to enzymatic activity and correlated with migration position on two-dimensional gels. Our results indicate that a group of basic polypeptides including proelastase, basic trypsinogen, basic chymotrypsinogen, and ribonuclease, two out of three forms of procarboxypeptidase B, and the major lipase species were greatly reduced or absent in tumor cell secretion. In contrast, the amount of acidic chymotrypsinogen was notably increased compared with normal acinar cells. Although the acinar tumor cells are highly differentiated cytologically and express functional receptors for several classes of pancreatic secretagogues, they show quantitative and qualitative differences when compared with normal pancreas with regard to their production of secretory proteins.
...
PMID:Biochemical analysis of secretory proteins synthesized by normal rat pancreas and by pancreatic acinar tumor cells. 618 2

We have previously established that secretory proteins from a rat acinar cell tumor lack two forms of procarboxypeptidase B, are deficient in a major lipase species, and possess markedly reduced amounts of the basic proteins proelastase, basic chymotrypsinogen, basic trypsinogen and ribonuclease (Iwanij, V., and J.D. Jamieson, J. Cell Biol., 95:734-741). Because secretory proteins are markers for acinar cell differentiation, we sought to establish whether the secretory protein profile of the acinar cell tumor is unique to the transformed cell or whether it resembles that of a stage of normal pancreatic development. To this end, we compared the secretory protein pattern from acinar tumor cells with that of rat pancreatic rudiments at days 19-22 of gestation and through day 21 of the postnatal period. Two-dimensional IEF-SDS gel electrophoresis coupled with biosynthetic labeling and fluorography indicates a time-dependent appearance of individual secretory proteins with basic polypeptides, except for amylase, appearing in the terminal stages of differentiation. In comparison, the secretory protein pattern of the acinar tumor cells most closely resembles that of day-19 embryonic pancreatic rudiments. We propose that the cells of the acinar cell tumor may, in part, mirror a stage of normal pancreatic development.
...
PMID:Comparison of secretory protein profiles in developing rat pancreatic rudiments and rat acinar tumor cells. 618 3


<< Previous 1 2 3 4 5 6 7 8 9 Next >>

---