Pancreatic RNase

2006 ◽  
Vol 2006 (1) ◽  
pp. pdb.rec8136
Keyword(s):  
Pancreatic Rnase

scholarly journals STUDIES ON THE FUNCTION OF INTRACELLULAR RIBONUCLEASES

1966 ◽  
Vol 29 (3) ◽  
pp. 395-403 ◽  
Author(s):  
Takeshi Utsunomiya ◽  
Jay S. Roth
Keyword(s):  
Natural Products ◽  
Sodium Chloride ◽  
Rat Liver ◽  
Messenger Rna ◽  
Rnase Activity ◽  
Optimum Ph ◽  
Normal Rat ◽  
Pancreatic Rnase ◽  
The Stability ◽  
Normal Constituent

The RNase activity and properties of ribosome and polysome preparations from normal rat liver and some hepatomas have been examined. Polysome and ribosome preparations from the Novikoff, McCoy MDAB, and Dunning hepatomas had considerably higher specific RNase activity than corresponding preparations from normal rat liver, Novikoff ascites, or Morris 5123 hepatomas. The optimum pH of the RNase was approximately 8.5 for all samples tested, and the samples showed no evidence of latent RNase activity when treated with 3 M sodium chloride, EDTA, urea, or p-chloromercuribenzenesulfonic acid. The RNase activity appeared to be associated principally with breakdown products and/or subunits smaller than 80S. In the presence of Mg++ ions, subunits could reaggregate to form monomer ribosomes indistinguishable from the natural products, but some of the reassociated ribosomes could contain RNase activity which had been bound to the smaller particles. Similar results were obtained with spermine. In the hepatomas, evidence was obtained for the preexistence of considerable amounts of the smaller, RNase-containing subunits in the cell. When a small amount of crystalline bovine pancreatic RNase was added to partly dissociated ribosomes, the RNase was found only in association with the smaller subunits, and little or no enzyme was taken up by ribosomes or polysomes. The results have led to the conclusion that RNase is not a normal constituent of the ribosome or polysome, but that RNase may become associated with these particulates if dissociation and reassociation take place. Some implications of these findings for the stability of messenger RNA and for the mechanism of its breakdown are discussed.

scholarly journals Evaluation of human pancreatic RNase as effector molecule in a therapeutic antibody platform

mAbs ◽  
2014 ◽  
Vol 6 (2) ◽  
pp. 367-380 ◽  
Author(s):  
Thomas Schirrmann ◽  
André Frenzel ◽  
Lars Linden ◽  
Beatrix Stelte-Ludwig ◽  
Jörg Willuda ◽  
...  
Keyword(s):  
Therapeutic Antibody ◽  
Effector Molecule ◽  
Pancreatic Rnase

scholarly journals Direct oxidation of polymeric substrates by multifunctional manganese peroxidase isoenzyme from Pleurotus ostreatus without redox mediators

2005 ◽  
Vol 386 (2) ◽  
pp. 387-393 ◽  
Author(s):  
Hisatoshi KAMITSUJI ◽  
Takashi WATANABE ◽  
Yoichi HONDA ◽  
Masaaki KUWAHARA
Keyword(s):  
Pleurotus Ostreatus ◽  
Manganese Peroxidase ◽  
Polymer Degradation ◽  
Veratryl Alcohol ◽  
Redox Mediators ◽  
Direct Oxidation ◽  
Peroxidase Isoenzyme ◽  
Pancreatic Rnase ◽  
Polymeric Substrates ◽  
Polymer Oxidation

VPs (versatile peroxidases) sharing the functions of LiP (lignin peroxidase) and MnP (manganese peroxidase) have been described in basidiomycetous fungi Pleurotus and Bjerkandera. Despite the importance of this enzyme in polymer degradation, its reactivity with polymeric substrates remains poorly understood. In the present study, we first report that, unlike LiP, VP from Pleurotus ostreatus directly oxidized two polymeric substrates, bovine pancreatic RNase and Poly R-478, through a long-range electron pathway without redox mediators. P. ostreatus produces several MnP isoenzymes, including the multifunctional enzyme MnP2 (VP) and a typical MnP isoenzyme MnP3. MnP2 (VP) depolymerized a polymeric azo dye, Poly R-478, to complete its catalytic cycle. Reduction of the oxidized intermediates of MnP2 (VP) to its resting state was also observed for RNase. RNase inhibited the oxidation of VA (veratryl alcohol) in a competitive manner. Blocking of the exposed tryptophan by N-bromosuccinimide inhibited the oxidation of RNase and VA by MnP2 (VP), but its Mn2+-oxidizing activity was retained, suggesting that Trp-170 exposed on an enzyme surface is a substrate-binding site both for VA and the polymeric substrates. The direct oxidation of RNase and Poly R by MnP2 (VP) is in sharp contrast with redox mediator-dependent oxidation of these polymers by LiP from Phanerochaete chrysosporium. Molecular modelling of MnP2 (VP) revealed that the differences in the dependence on redox mediators in polymer oxidation by MnP2 (VP) and LiP were explained by the anionic microenvironment surrounding the exposed tryptophan.

scholarly journals Direct association of messenger RNA labeled in the presence of fluoroorotate with membranes of the endoplasmic reticulum in rat liver.

1976 ◽  
Vol 70 (1) ◽  
pp. 47-58 ◽  
Author(s):  
J Cardelli ◽  
B Long ◽  
H C Pitot
Keyword(s):  
Endoplasmic Reticulum ◽  
Ribosomal Rna ◽  
Messenger Rna ◽  
Translational Regulation ◽  
Orotic Acid ◽  
Complete Removal ◽  
High Ionic Strength ◽  
Messenger Rnas ◽  
Direct Association ◽  
Pancreatic Rnase

Liver rough endoplasmic reticulum (RER) membranes were isolated from rats given [3H]orotic acid for 48 h (ribosomal RNA [rRNA] label) or for 3 h along with 5-fluoroorotate; this latter procedure permits the labeling of cytoplasmic messenger RNAs (mRNAs) in the absence of rRNA labeling. More than 50% of the labeled mRNA remained attached to membranes of the RER after complete removal of ribosomes with a buffer of high ionic strength in the presence of puromycin. Under similar conditions, membranes retained 40% of their polyadenylate as determined by a [3H]-polyuridylate hybridization assay. Treatment of mRNA-labeled endoplasmic reticulum membranes with pancreatic RNase indicates that the polyadenylate and possibly nonpolyadenylate-pyrimidine portions of the messenger are involved in the binding of mRNA to the membranes. The implication of these results in furthering our understanding of the mechanisms of the translational regulation of genetic expression is discussed.

Cloning and cytotoxicity of a human pancreatic RNase immunofusion

1997 ◽  
Vol 3 (2) ◽  
pp. 127-136 ◽  
Author(s):  
Monika Zewe ◽  
Susanna M Rybak ◽  
Stefan Dübel ◽  
Johannes F Coy ◽  
Martin Welschof ◽  
...  
Keyword(s):  
Pancreatic Rnase

Three-dimensional domain swapping and supramolecular protein assembly: insights from the X-ray structure of a dimeric swapped variant of human pancreatic RNase

2013 ◽  
Vol 69 (10) ◽  
pp. 2116-2123 ◽  
Author(s):  
Andrea Pica ◽  
Antonello Merlino ◽  
Alexander K. Buell ◽  
Tuomas P. J. Knowles ◽  
Elio Pizzo ◽  
...  
Keyword(s):  
Three Dimensional ◽  
Supramolecular Assembly ◽  
Domain Swapping ◽  
Crystallographic Axis ◽  
Force Microscopy ◽  
Atomic Force ◽  
Pancreatic Rnase ◽  
Quaternary Structures ◽  
New Evidence ◽  
Dimensional Domain

The deletion of five residues in the loop connecting the N-terminal helix to the core of monomeric human pancreatic ribonuclease leads to the formation of an enzymatically active domain-swapped dimer (desHP). The crystal structure of desHP reveals the generation of an intriguing fibril-like aggregate of desHP molecules that extends along theccrystallographic axis. Dimers are formed by three-dimensional domain swapping. Tetramers are formed by the aggregation of swapped dimers with slightly different quaternary structures. The tetramers interact in such a way as to form an infinite rod-like structure that propagates throughout the crystal. The observed supramolecular assembly captured in the crystal predicts that desHP fibrils could form in solution; this has been confirmed by atomic force microscopy. These results provide new evidence that three-dimensional domain swapping can be a mechanism for the formation of elaborate large assemblies in which the protein, apart from the swapping, retains its original fold.

Immunological studies of ribonuclease C from human urine.

1981 ◽  
Vol 27 (8) ◽  
pp. 1362-1367 ◽  
Author(s):  
J W Cranston ◽  
H C Hoover ◽  
E R Crisp
Keyword(s):  
Pancreatic Carcinoma ◽  
Human Urine ◽  
Rnase A ◽  
Serum Samples ◽  
Positive Correlation ◽  
Alternative Method ◽  
Normal Individuals ◽  
Human Sera ◽  
Pancreatic Rnase

Abstract Antiserum to human urinary RNase C [ribonuclease (pancreatic), EC 3.1.27.5], developed in rabbits, was used to characterize this enzyme through studies of inhibition of RNase C-catalyzed poly(C) hydrolysis and of competition in a RIA. By either assay, the antiserum failed to cross react with human urinary RNase U (EC 3.1.27.-) or bovine pancreatic RNase A (EC 3.1.27.5). RNase C is immunologically identical to the poly(C)-active RNase in various human sera, including samples obtained from normal individuals, patients with pancreatic carcinoma, pancreatitis, or other malignant and nonmalignant diseases. This conclusion is based on the finding of superimposable antibody dose-inhibition curves for poly(C) hydrolysis and parallel competition RIA curves for RNase C and the various sera. There was a positive correlation (r = 0.73; p less than 0.001) between concentrations of RNase C as determined by poly(C) hydrolysis and competition RIA in serum samples from 102 patients. Therefore, the latter technique provides al alternative method for measuring RNase C in sera.

Quelques aspects de la synthèse protéique dans les muscles thoraciques en développement de Schistocerca gregaria (Forsk.)

1972 ◽  
Vol 50 (11) ◽  
pp. 1226-1237 ◽  
Author(s):  
C. Richard ◽  
K. D. Chaudhary
Keyword(s):  
Amino Acid ◽  
Schistocerca Gregaria ◽  
Combined Treatment ◽  
Treatment Result ◽  
Amino Acid Incorporation ◽  
Acid Incorporation ◽  
A Cell ◽  
Rnase Treatment ◽  
Thoracic Muscles ◽  
Pancreatic Rnase

Polysomes obtained from the postmitochondrial fraction of the thoracic muscles undergo disassociation into monomers when treated with pancreatic RNase. In contrast, the preparations obtained from microsomes on RNase treatment result in the association of monomers into heavier aggregates. A combined treatment with trypsin, however, renders the polysomes sensitive to RNase action. Characteristics of a cell-free amino acid incorporation system have been described and compared with similar systems obtained from other organisms or tissues. GTP seems to reverse the inhibition caused by cycloheximide. Amino acid incorporation capacity of the microsomal and ribosomal fractions prepared from the thoracic muscles at different stages of development was investigated in the presence and absence of added poly U. Both the microsomal and ribosomal preparations respond to the addition of poly U. However, the ribosomes require higher concentrations of this copolymer for attaining full saturation. The significance of the findings reported in this investigation is discussed.

A proposed nucleotide sequence for the 5S ribosomal ribonucleic acid of rainbow trout (Salmo gairdneri)

1978 ◽  
Vol 56 (1) ◽  
pp. 60-65 ◽  
Author(s):  
Kenneth L. Roy
Keyword(s):  
Rainbow Trout ◽  
Nucleotide Sequence ◽  
Ribonucleic Acid ◽  
Gel Electrophoresis ◽  
Inorganic Phosphate ◽  
Polyacrylamide Gel Electrophoresis ◽  
Salmo Gairdneri ◽  
Ribosomal Ribonucleic Acid ◽  
Complete Digestion ◽  
Pancreatic Rnase

Rainbow trout cell cultures have been exposed to 32P-labelled inorganic phosphate and the labelled RNA has been isolated. The 5S ribosomal ribonucleic acid (5S rRNA) was purified by polyacrylamide gel electrophoresis, then digested with RNase T1 or pancreatic RNase. The products of complete digestion were separated and their sequences determined. These analyses have allowed a sequence to be proposed which differs in eight positions from that of mammalian 5S rRNAs.

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