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)

Using specific antirenal sera obtained from rabbits and absorbed with a mixture of extracts from heterologous organs, a specific antigen was detected in human and CBA mouse renal extracts. Its molecular weight was found to amount to about 100 000 dalton. It is salted out with ammonium sulfate at 50-70% saturation of renal extract and is destroyed on extract heating for 30 min at 75 degrees C. This antigen is sensitive to trypsin and papain but resistant to hyaluronidase. It is partially destroyed by DNase and RNase, provided the latter ones are used in comparatively high doses (1 mg per 0.3 ml extract) and exposure lasts one day. Based on the study of the physicochemical properties it is suggested that the kidney-specific antigen may be a ribonucleoprotein or a deoxyribonucleoprotein but cannot be attributed to glycoproteins.
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PMID:[Physicochemical properties of kidney-specific antigen]. 669 26

The presence of glycosaminoglycans (GAG) has been histochemically demonstrated in the CNS of various mammalian species. They have been related with some nerve functions as neurotransmitters storage and synaptic transmission. In the present paper, the histochemical properties of nerve cell cytoplasmic GAG were studied in several regions of adult human CNS. Samples of brain cortex, pons, upper medulla, and cerebellar cortex obtained by autopsy from subjects not dying after neurological diseases were fixed by immersion in glutaraldehyde, dehydrated with ethanol, and embedded in paraffin. The sections were stained with Alcian blue solutions adjusted to pH 2.5, 4.0, and 5.7. To the latter solution MgCl2 was added in increasing concentration from 0.05 to 1.2 M. Testicular hyaluronidase, neuraminidase, and ribonuclease were applied on simultaneous sections with their respective controls. The sequence of these reactions allowed us to demonstrate the presence of hyaluronic acid along chondroitin-4- and/or 6-sulphate in the cytoplasm of most nerve cells. The sulphated GAG showed certain variability in the various regions studied related specially with their grade of sulphation.
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PMID:Histochemical demonstration of cytoplasmic glycosaminoglycans in the macroneurons of the human central nervous system. 670 30

An enzymatic profile of 20 strains of Pseudomonas maltophilia was undertaken with conventional plate tests, API ZYM, and 4-methylumbelliferyl-conjugated substrates. All strains produced DNase, RNase, arbutinase, esterases and lipases, mucinase, acid and alkaline phosphatases, alkaline pyrophosphate diesterase, phosphoamidase, beta-glucosidase, leucine arylamidase, and acetatase and were hemolytic for horse, sheep, and rabbit blood. The majority of strains produced chitinase, hyaluronidase, albuminase, valine arylamidase, trypsin, alpha- and beta-glucosidases, and N-acetyl-beta-glucosaminidase. API ZYM and 4-methylumbelliferyl-conjugated substrate assays are rapid, simple, specific, and sensitive and may be useful as diagnostic aids in the identification of P. maltophilia and other pseudomonads.
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PMID:Enzymatic profile of Pseudomonas maltophilia. 681 50

Rat liver nuclear matrix and similar structures derived from isolated Chironomus polytene chromosomes, nuclear envelopes, and intranuclear bodies of frog late oocytes (the karyospheres) were studied by electron microscopy with platinum shadowing and negative staining. We have shown that the treatment of whole nuclei, nuclear envelopes, polytene chromosomes, or karyospheres with nonionic detergent, high salt, and RNase and DNase followed by dilute alkali or hyaluronidase digestion reveals numerous rather uniform granules 25-30 nm in diameter. With omission of the nucleases the granules appear to be associated with DNA strands mostly organized in loops. Many granules form clusters and are arranged in linear or arch-like aggregates or cycles resembling the pore complexes. We suppose that these spherical bodies constitute a basic component of the nuclear matrix, chromosome scaffold, and nuclear envelope and are bound together by hyaluronic acid or some similar glycosaminoglycan.
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PMID:Granules 25-30 nm in diameter: basic constituent of the nuclear matrix, chromosome scaffold, and nuclear envelope. 696 Mar 56

An approximately 50-fold increase in serum beta-glucuronidase activity appeared 2 hours after the administration of such organophosphate insecticides as dichlorvs, diazinon and disulfoton and of a carbamate insecticide, carbaryl. The activities of other acid hydrolases in the serum such as ribonuclease, acid phosphatase, hyaluronidase and N-acetylglucosaminidase did not change significantly after the insecticide treatment. The response was related to the dose level and was evident after a single intraperitoneal dose of diazinon as low as 1.6 mg/kg. This appearence of an increase in beta-glucuronidase was retarded by pretreatment with SKF 525A, an inhibitor of drug metabolizing enzyme. When beta-glucuronidase was elevated by a large dose of diazinon, full response to a second dose of diazinon did not occur until approximately one month after administration of the first dose.
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PMID:Increase of beta-glucuronidase activity in the serum of rats administered organophosphate and carbamate insecticides. 726 27

A method has been developed which allows the analysis of glycoproteins separated by SDS-PAGE. The procedure, though applicable to N-glycosylated glycoproteins of any origin, is particularly devised for glycoproteins potentially containing fucose in alpha1,3-linkage to the reducing GlcNAc as may be found in plants and invertebrates, e.g., insects and parasitic helminths. Starting with an established procedure for mass spectrometric peptide mapping, the analysis of N-glycans by matrix-assisted laser desorption/ionization mass spectrometry involved the use of peptide:N-glycosidase A, a triphasic microcolumn for sample cleanup, and a new matrix mixture consisting of 2,5-dihyhydroxybenzoic acid, 1-hydroxyisoquinoline, and arabinosazone. The method was tested on proteins with N-glycans of known structure, i.e., as horseradish peroxidase, zucchini ascorbate oxidase, soybean agglutinin, honeybee venom hyaluronidase, bovine ribonuclease B, and bovine fetuin. An electrophoretic band corresponding to 4 microg of glycoprotein was generally sufficient to allow detection of the major N-glycan species. As an additional benefit, a peptide mass map is generated which serves to identify the analyzed protein. The method was applied to glycoprotein allergens whose glycan structures were unknown. Ara h 1 and Ole e 1, major allergens from peanut and olive pollen, respectively, contained mainly xylosylated N-glycans with the composition Man(3(-4))XylGlcNAc(2) in the case of Ara h 1 and GlcNAc(1-2)Man(3)XylGlcNAc(2) in the case of Ole e 1 where also some GlcNAc(0-2)Man(3)XylFucGlcNAc(2) was found.
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PMID:N-Glycan analysis by matrix-assisted laser desorption/ionization mass spectrometry of electrophoretically separated nonmammalian proteins: application to peanut allergen Ara h 1 and olive pollen allergen Ole e 1. 1099 64

Sperm adhesion molecule 1 (Spam1) is a widely conserved sperm surface protein with multiple roles in mammalian fertilization. Although the gene for this protein has been thought to be testis specific based on Northern blot analysis, there is evidence for nontesticular expression when transcripts are analyzed by more sensitive techniques. In the present investigation, results of a reverse transcription polymerase chain reaction assay, an RNase-protection assay (RPA), and an in situ transcript hybridization assay revealed that the murine Spam1 gene is transcribed in the female genital tract. RPA revealed that Spam1 transcripts are synthesized in a region-dependent manner, with the oviduct having lower transcript levels than the uterus and vagina. The transcripts levels were 3- to 10-fold lower in the female genital tract than in the testis. In situ transcript hybridization assay revealed RNA in the luminal epithelium in all three regions of the genital tract and in the uterine myometrium and the oviductal mesothelium. Western blot analysis and immunohistochemistry demonstrated that the protein concentration is 1.5- to 3-fold lower in female tissues than in sperm, and localization is similar to that of the transcripts. The protein has hyaluronidase activity at neutral pH, which is unique for sperm hyaluronidase, but not at acidic pH. In the uterus, Spam1 expression fluctuated during the estrous cycle. Its localization suggests that in addition to functioning as a secretory protein, it may be involved in hyaluronic acid metabolism or turnover in the female genital tract. Our results provide further evidence that Spam1 is a multifunctional protein and that it is less restricted in its expression than previously reported.
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PMID:Mouse Spam1 (PH-20) is a multifunctional protein: evidence for its expression in the female reproductive tract. 1267 66

Beining, Paul R. (The Catholic University of America, Washington, D.C.) and E. R. Kennedy. Characteristics of a strain of Staphylococcus aureus grown in vivo and in vitro. J. Bacteriol. 85:732-741. 1963.-A comparative survey was conducted on the characteristics of a strain of Staphylococcus aureus after it had been grown in vitro (VSB) and after it had been collected from the peritoneal exudate of an infected guinea pig (GSB). Both VSB and GSB strains gave the same results when studied in an extensive series of tests, including bound and soluble coagulases, bacteriophage type, antibiotic-sensitivity pattern, the usual fermentation reactions, deoxyribonucleic acid base composition, and qualitative tests for hemolysins, deoxyribonuclease, ribonuclease, staphylokinase, staphyloprotease, lipase, and phosphatase. The in vivo strain differed significantly from the in vitro strain in respiratory rate, agar gel diffusion studies, agglutinability in tube tests, virulence tests in rabbits and mice, growth on tellurite-glycine agar, susceptibility to human gamma-globulin in agar, and in the quantitative production of deoxyribonuclease, alpha-hemolysin, leucocidin, and hyaluronidase.
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PMID:CHARACTERISTICS OF A STRAIN OF STAPHYLOCOCCUS AUREUS GROWN IN VIVO AND IN VITRO. 1404 37

This report demonstrates that a single set of identical synthetic multifunctional pores can detect the activity of many different enzymes. Enzymes catalyzing either synthesis or degradation of DNA (exonuclease III or polymerase I), RNA (RNase A), polysaccharides (heparinase I, hyaluronidase, and galactosyltransferase), and proteins (papain, ficin, elastase, subtilisin, and pronase) are selected to exemplify this key characteristic of synthetic multifunctional pore sensors. Because anionic, cationic, and neutral substrates can gain access to the interior of complementarily functionalized pores, such pores can be the basis for very user-friendly screening of a broad range of enzymes.
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PMID:Enzyme screening with synthetic multifunctional pores: focus on biopolymers. 1453 Apr 13

Subcutaneous application of bovine RNase A conjugated to HYase (bovine hyaluronidase), polyethylene glycol (PEG) and HYase+PEG resulted in a marked reduction of the width of the spermatogenic layers of the mouse testes. The number of sperms in caput epididymidis was significantly decreased in mice injected with conjugated RNase A. There was not any significant embryotoxic effect of free RNase A even conjugated with HYse, PEG and HYse+PEG. The immunogenicity, expressed in production of antibodies against free RNase A or conjugates with PEG, was very low. However, the immunogenic action of this enzyme conjugated only to HYase was much higher and produced the same immunogenicity as HYase itself. The immunogenic effect of RNase A+HYase conjugate decreased when PEG was joined to this conjugate. The inhibitory effect of RNase A conjugated to HYase, PEG and HYase+PEG on human ML-2 cells studied in vitro, was practically ineffective. On the other side, when RNase A conjugated to HYase or PEG was administered intraperitoneally into the mice bearing human melanoma, the antitumor effect was pronounced.
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PMID:Effect of hyaluronidase and PEG chain conjugation on the biologic and antitumor activity of RNase A. 1474 90


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