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:3.1.27.4 (ribonuclease)
6,621 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A folate-binding protein (binder) from human choroid plexus was solubilized with Triton X-100 and partially purified in three steps: (1) affinity chromatography, (2) Sephadex G-200 column chromatography, and (3) polyacrylamide gel electrophoresis. When the partially purified binder was subjected to sodium dodecyl sulfate--polyacrylamide gel electrophoresis, the binding activity was located in the region of the gel with a molecular weight between 45,000 and 60,000. The specific activity of the binder after the three purification steps was 1.2 mu g folic acid/mg protein, a 316-fold purification. Binding activity of the partially purified binder decreased below pH 6.0 and above pH 8.0, was unaffected by treatment with ribonuclease or deoxyribonuclease, but was abolished with trypsin, chymotrypsin, or protease (Streptomyces griesus). The binding of folic acid to the human binder was inhibited by folate Greater Than H4-folate Greater Than methyl-H4-folate approximately dihydrofolate approximately pteroic acid Greater Than methotrexate approximately aminopterin.
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PMID:Partial purification and characterization of a folate-binding protein from human choroid plexus. 727 9

The effect of prolactin on the digestive potency of the acinar pancreas was examined in pituitary-grafted hyperprolactinemic mice, because our previous experiment showed that a marked proliferation of pancreatic acinar cells was induced by pituitary grafting in mice. To know whether the digestive function is modified, the tissue contents of pancreatic digestive enzymes, such as chymotrypsin, lipase alpha-amylase and ribonuclease, were measured in the hyperprolactinemic mice. Pituitary grafting significantly increased the contents of chymotrypsin and lipase in the pancreas on day 12 after the operation without affecting intake of food, when compared to those in the sham-operated controls. On day 30, however, the differences between pituitary-grafted and control mice were no more discernible. Thus, the digestive enzyme activities are easily modified soon after the increase of circulating prolactin level. This effect of prolactin on the function of the pancreas may be responsible for "homeorhetic" control of nutrients during lactation. In another set of experiments in adrenalectomized-castrated or castrated mice, pituitary grafting induced an increase in the weight of the pancreas. In addition, adrenalectomy in combination with castration did not alter the pancreatic contents of chymotrypsin and lipase but decreased the amylase content. These results taken together seem to indicate that the effect of prolactin on the exocrine pancreas is not mediated by gonadal and adrenal steroid hormones.
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PMID:Modification of pancreatic digestive function by pituitary grafting in mice. 765 48

The percentage of bacteriocin-producing and phage-producing Klebsiella strains was as follows: K. pneumoniae-10%, K. ozaenae-7%, K. rhinoscleromatis-9%. The antimicrobial spectrum of the studied inducible particler was broad and was not limited by the frames of the genus and family. Bacteriocins and bacteriophages from Klebsiella were active to Klebsiella, Enterobacter, Escherichia, Shigella and Proteus representatives significant in medicine. Klebocins and Klebsiella phages exhibited antagonistic effects to phytopathogenic bacteria. Some strains of Erwinia and Pseudomonas were sensitive to phages or bacteriocins from Klebsiella. Bacteriocins protected corn and tomato seeds from contamination by erwinioses agents. All cultures of Agrobacterium, Corynebacterium, Micrococcus, Staphylococcus, Streptococcus were resistant to action of phages and klebocins. Bacteriocins from Klebsiella were assayed for their sensitivity to trypsin, chymotrypsin, lysozyme, ribonuclease, deoxyribonuclease. Action of klebocins was associated with a protein component. Proceeding from data of diffusion through the disc ultrafiltration membranes molecular weight of klebocins was in the range of 30,000 and 50,000 Da.
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PMID:[The antimicrobial spectrum of the action of bacteriocins and bacteriophages from Klebsiella strains]. 816 98

Prior studies have revealed the presence of chymotrypsinlike protease in peripheral organs, although no definitive evidence for the synthesis of this enzyme in tissue other than the pancreas is available. In an attempt to detect chymotrypsinogen mRNA in peripheral organs, a fragment of the pancreatic chymotrypsin mRNA from rat was amplified using PCR. The sequence was identified as a portion of the rat chymotrypsin B gene overlapping exon 5 through exon 7. It was subcloned into the pGEM-4Z vector and used as a template for the vitro transcription of an antisense riboprobe. Using ribonuclease protection and Northern blot analyses, chymotrypsin mRNA was detected in the rat pancreas, stomach, duodenum, ovary, and spleen. Monoclonal and polyclonal antisera against chymotrypsin detected chymotrypsinlike immunoreactivity in rat and human pancreas, rat stomach, duodenum and jejunum. Electrophoresis and immunoblotting revealed chymotrypsin-chymotrypsinogen bands (25-29 kDa) in the stomach and duodenum. Synthesis of a potent protease such as chymotrypsin in tissue other than pancreas is significant, suggesting a potential physiological and/or pathological role in these tissues.
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PMID:Chymotrypsin gene expression in rat peripheral organs. 956 Apr 77

A quick and simple method has been developed for the recovery of proteins from water-in-oil microemulsions (w/o-MEs), which is needed to further the use of liquid-liquid extraction in bioseparations. By adding a small portion (0.1 v/v or less) of cosurfactant (e.g., 1-alkanol) to w/o-ME solution, proteins were readily expelled, sometimes as solids, while most or all of the surfactant (Aerosol OT) remained in solution. The release of proteins increased with the further addition of cosurfactant and was greater when the molar ratio of protein to w/o-ME or fractional occupancy (f) was high. However, protein expulsion was also significant when f was small. The addition of cosurfactant released ribonuclease, lysozyme, alpha-chymotrypsin, pepsin, bovine serum albumin (BSA), and catalase from w/o-ME solution, but the expulsion was greater for BSA relative to chymotrypsin and lysozyme. Protein expulsion also increased with cosurfactant chain length for the homologous series of 1-alkanols starting at 1-butanol; however, water was also coexpelled in significant amounts. An exception to the latter rule was 1-butanol, which readily promoted the release of protein, but not encapsulated water. The addition of 1-butanol to a w/o-ME solution containing alpha-chymotrypsin and BSA selectively released the former protein, with chymotryptic activity occurring in the recovered protein. Possible mechanisms for the cosurfactant-mediated release of protein are discussed. Copyright 1998 John Wiley & Sons, Inc.
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PMID:Expulsion of proteins from water-in-oil microemulsions by treatment with cosurfactant 1009 72

Alkyl-substituted hydroxybenzenes (AHBs), auto-inducers of microbial dormancy (or d1 factors), were found to stabilize the structure of protein macromolecules, making them metabolically less active and more resistant to stresses. In vitro experiments with the Bacillus intermedius ribonuclease and chymotrypsin showed that the degree of the physical and chemical stability of these enzymes treated with AHBs depends on their concentration and incubation time. Experiments with RNase, which is capable of refolding, i.e., renaturation after heat denaturation, revealed that AHBs efficiently interact with both intact and denatured proteins. The data obtained allow the inference to be made that d1 factors may play the role of natural chemical chaperons, blocking metabolism in dormant cells through the formation of catalytically inactive thermostable complexes with enzymes.
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PMID:[Stabilization of enzymes by anabiosis autoinducers as a possible mechanism of resistance of resting microbial forms]. 1077 22

Further studies on fever production by injection of leukocyte extracts or cell-free supernatant fluids from peritoneal exudates in rabbits are reported. Granulocytes collected from peripheral blood or from pleural exudates contain a heat-labile pyrogenic substance. The material in extracts of leukocytes and in peritoneal fluids, which causes fever, is destroyed by heating for 30 minutes at 90 degrees C. at pH 7.2 and at 70 degrees C. at pH 4.5. It is active in producing fever over a pH range of 2.0 to 10.5 and maintains potency for as long as 6 months at 4 degrees C. The fever-producing substance in leukocyte extracts is not dialyzable. Its activity is not destroyed by trypsin, chymotrypsin, or ribonuclease. No evidence of plasma activator or inhibitor was detected. Significant temperature elevation in the rabbit was effected by a quantity of leukocyte extract containing 0.76 mg. protein and 0.054 mg. polysaccharide. The febrile response produced by the material under study was compared with that of Menkin's pyrexin as well as with that of bacterial pyrogens. Several significant differences were noted. The properties of pyrexin are similar to those of bacterial pyrogens. Amidopyrine suppressed the febrile response to injection of leukocyte extracts, whereas neither amidopyrine nor cortisone influenced the appearance of pyrogenic material in induced peritoneal exudates. Peritoneal fluids collected from rabbits made leukopenic by HN(2) were found to contain a fever-promoting substance. Its character has yet to be determined. It is concluded that there is present in polymorphonuclear leukocytes of rabbits a heat-labile factor capable of producing fever in rabbits and that the leukocyte is probably not the only source of such a factor.
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PMID:Studies on the pathogenesis of fever. II. Characterization of fever-producing substances from polymorphonuclear leukocytes and from the fluid of sterile exudates. 1310 5

1. The hemagglutinating capacity, enzymic activity, and infectivity of several influenza viruses were destroyed by repeated freezing and thawing of dialyzed allantoic fluids containing them. 2. Influenza virus degraded by freezing and thawing, by treatment with 5 M urea, or by heating at 65 degrees C. still combined with homologous antibody and was demonstrable by blocking of the hemagglutination-inhibition and virus neutralization reactions. 3. After 50 cycles of freezing and thawing, much of the blocking antigen activity was not sedimented by centrifugation at 120,000 g for 2 hours, and electron microscopy showed complete disruption of the virus particles. So called soluble blocking antigen was obtained from four strains of influenza A, the Lee strain of influenza B, mumps, and Newcastle disease viruses. 4. Soluble blocking antigens from influenza A viruses were highly strain-specific; gave little or no reaction in complement-fixation tests; stimulated but little antibody production in rabbits and did not induce immunity in mice; caused reactivation of infective virus in neutral mixtures of homologous virus and immune serum. 5. Repeatedly frozen and thawed influenza virus preparations did not interfere with the propagation of infective virus in the allantoic sac. The blocking antigen activity they contained was precipitated by half saturated ammonium sulfate, destroyed by trypsin, chymotrypsin, or heating at 56 degrees C. for 30 minutes, but was unaffected by desoxyribonuclease or ribonuclease. 6. These findings are in accord with the view that soluble blocking antigen obtained from influenza virus particles on disruption by repeated freezing and thawing is protein in nature and represents the essential antigenic material of the intact virus.
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PMID:Disruption of influenza virus; properties of degradation products of the virus particle. 1315 79

Lambda coli phage is not inactivated by chymotrypsin, trypsin, or ficin. T(2) phage is slowly inactivated by high concentrations of (alpha-, beta-, gamma-, or Delta-chymotrypsin, but not by trypsin or ficin. P(1) phage is slowly inactivated by alpha-, beta-, or gamma-chymotrypsin, or ficin, more rapidly by Delta-chymotrypsin, and much more rapidly by trypsin. Crystalline egg albumin, crystalline serum albumin, E. coli nucleoprotein, and yeast nucleoprotein are hydrolyzed slowly by alpha-chymotrypsin. Yeast nucleoprotein, like P(1) phage, is hydrolyzed more rapidly by Delta-chymotrypsin than by alpha-chymotrypsin, but not by trypsin or ficin. Neither phages nor native proteins were attacked by papain, carboxypeptidase, deoxyribonuclease, or ribonuclease.
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PMID:THE EFFECT OF PROTEOLYTIC ENZYMES ON E. COLI PHAGES AND ON NATIVE PROTEINS. 1421 51

Agglutinability of human erythrocytes for 3 hemagglutinating adenoviruses was markedly reduced by pretreatment of red cells with a factor present in tissue cultures which had been infected with adenovirus types 1, 2,4, or 15. The factor responsible for erythrocyte receptor modification was non-dialyzable and unaffected by the action of ribonuclease, desoxyribonuclease, trypsin, chymotrypsin, or ether. The factor was smaller, more thermostable, and separable from the infectious virus. Erythrocyte receptor modification was found to be a function of time and temperature. Titers of erythrocyte receptor-modifying activity were not diminished by successive exposures to fresh erythrocytes. Erythrocytes treated with erythrocyte receptor-modifying factor suspensions failed to significantly adsorb test virus hemagglutinin. Inhibition of erythrocyte receptor modifying-activity of the adenovirus suspensions by rabbit antiserum was type-specific.
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PMID:Further characterization of the adenovirus erythrocyte receptor-modifying factor. 1445 30


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