Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
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Gene/Protein
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Target Concepts:
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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)
Circulating M antigen, specific for genus Schistosoma, was previously described in serum, urine, patients' milk, and in serum and urine of animals infected by S. mansoni. The M antigen was thermostable and soluble in trichloroacetic acid. It was not hydrolyzed by protease,
ribonuclease
, amylase, or
neuraminidase
but destroyed by sodium metaperiodate. In the present study, we have purified the M ag by using trichloroacetic acid solubility, DEAE Sephadex, and immunoadsorption. The M ag showed a neutral electric charge, a m.w. heterogeneity, and was only stained by periodic acid-Schiff. The composition study revealed M ag was a glycoprotein with a polysaccharide moiety (63% of the molecules) particularly rich in galactose, fucose, glucosamine, and mannose, and with a high molecular ratio of serine and threonine. The presence of O-glycosidic linkage allowed M ag to be considered as a mucin or a mucus glycoprotein-like component. It was localized in the cell wall of the gut of adult worms.
...
PMID:Purification, immunochemical, and biologic characterization of the Schistosoma circulating M antigen. 698 17
The two major
ribonuclease
(
EC 3.1.27.5
) present in normal human urine have been highly purified and extensively characterized for their enzymatic, physical, chemical and structural properties. One of the enzymes, RNAase C, is a glycoprotein which exhibits a pH optimum of 8.5 with RNA as the substrate and preferentially degrades the synthetic homoribopolymer poly(C). This enzyme is resolved into multiple components by column electrofocusing. However, prior treatment with
neuraminidase
results in a single form of RNAase C with an isoelectric point of 10.4, indicating that the charge heterogeneity is the result of variability in sialic acid content. Amino acid composition and NH2- and COOH-terminal sequence analyses of RNAase C show that this enzyme is very similar to mammalian pancreatic RNAases; the data indicate a peptide chain of 126 amino acid residues and a 33% carbohydrate content. The second enzyme isolated from urine, termed RNAase U, is also a glycoprotein which has a pH optimum of 7.0 with RNA as substrate and is virtually inactive against poly(C). RNAase U lacks sialic acid and focuses as a single component with a highly basic isoelectric point of greater than pH 11.0. The NH2- and COOH-terminal sequences of RNAase U show little homology with the pancreatic RNAases. However, the amino acid composition of this enzyme indicates it is very similar to human spleen RNAase.
...
PMID:Purification and properties of ribonucleases from human urine. 721 38
By using a suckling mouse assay, heat-stable enterotoxin (ST) was purified from the culture filtrate of Yersinia enterocolitica isolated from a diarrheal patient. The purification procedures involve ultrafiltration with an Amicon HIP-10 hollow fiber, ethanol fractionation, protamine sulfate treatment, diethylaminoethyl-Sephacel and hydroxylapatite column chromatographies, and Sephacryl S-200 superfine gel filtration. About 408-fold purification was achieved, with a yield of 12.0%. The minimal effective dose of purified ST was about 110 ng in the suckling mouse assay. The molecular weight of purified ST was 9,000 by Sephadex G-100 superfine gel filtration. The purified ST was stable to heating (100 degrees C for 20 min, 121 degrees C for 20 min) and did not lose its toxicity after treatment with protease, trypsin, lipase, phospholipase C,
ribonuclease
, deoxyribonuclease, beta-glucosidase, and
neuraminidase
. The purified ST was separated by isoelectric focusing into two active fractions, with pI's of 3.29 (ST-1) and 3.00 (ST-2), respectively. Antiserum from guinea pigs immunized with the purified ST neutralized the activity of both Y. enterocolitica ST and Escherichia coli ST.
...
PMID:Partial purification and characterization of heat-stable enterotoxin produced by Yersinia enterocolitica. 721 60
The role of cell surface charge in cellular interactions has been the subject of conflicting reports. The major contribution to the net cell surface negativity of all mammalian cells studied is made by the sialic acid moieties of the surface glycoproteins, while
ribonuclease
-susceptible sites have been shown to contribute to the lesser extent on some cell types. Experiments were done to determine whether these anionic groups at the cell periphery affect the aggregation and sorting behaviour of embryonic chick neural retina cells when cultured alone or in combination with embryonic heart cells. The net negative surface charge density, as determined by cell electrophoretic mobility, of
neuraminidase
- or
ribonuclease
-treated cells was significantly decreased immediately after incubation with the enzymes, and the treatment with
neuraminidase
resulted in a reduction in the binding of colloidal iron hydroxide particles at the cell surface. Both enzymes caused reduced aggregate size in gyratory shaker cultures of neural retina and mixed cell suspensions, and fewer neural retina cells adherent to microtest plate surfaces, but no differences were seen in their histological appearance or sorting pattern in mixed shaker culture. The results indicate that the
neuraminidase
- and
ribonuclease
-susceptible groups at the periphery of embryonic neural retina cells play a role in some aspects of cell contact behaviour in ways other than reduction in net negative surface charge.
...
PMID:The effect of neuraminidase- and ribonuclease-susceptible surface anionic groups on the aggregation of embryonic chick neural retina cells. 732 84
By molecular hybridization and by
neuraminidase
inhibition tests it is shown that all influenza A strains tested carrying an Nav3 or Nav2
neuraminidase
(NA) are genetically highly related in their NA genes and cross-react serologically with specific antineuraminidase sera. The Nav6 strains exhibit a very low
RNase
protection after hybridization and do not cross-react serologically with Nav2 or Nav3 strains. Thus, the Nav2 and Nav3 strains comprise one group which is distinct from that of Nav6 strains.
...
PMID:Genetic relatedness of the neuramindase of influenza A strains Nav2, Nav3, and Nav6. 741 73
Antigens A and B, shown to be associated with the progestagen-dominated human endometrium, were partly purified and their properties studied. The antigens were recovered in the crude nuclei, the heavy particulate fraction and cytosol of decidua-rich tissue from early pregnancy. The antigens in cytosol were enriched by a combination of Concanavalin A-Sepharose chromatography and polyacrylamide gel electrophoresis. The immunological reactivity of the antigens after partial purification by Concanavalin A-Sepharose chromatography was retained after 30 min exposure to 4-85 degrees C at pH 7.4, or after 2 h to pH 2-12 at 22 degrees C. Trypsin, but not pepsin,
RNase
, DNase or
neuraminidase
, completely destroyed immunological reactivity of both antigens. The apparent molecular weight of both antigens determined by filtration on Sephadex G100 was 48 000. The isoelectric point of both antigens was approximately 4.9. The antigens were not immunologically related to transferrin, ceruloplasmin, alpha-1-antitrypsin, ferritin, uteroglobin, alpha-fetoprotein, human chorionic gonadotrophin, pregnancy-associated plasma proteins or pregnancy zone protein. Furthermore, the antisera to Antigens A and B did not react with the decidual cytosol of pregnant baboons or of pseudopregnant rats.
...
PMID:Properties of the progestagen-dependent protein of the human endometrium. 743 Dec 86
Electrophoretic mobility, glucose metabolism, and oxygen uptake were studied in three leukemic and in four nonleukemic strains of ascites tumor cells. The cells differed markedly in mobility. This variation was related neither to cell growth nor to rates of endogenous respiration and aerobic glycolysis. The nonleukemic tumor cells showed higher mobility than did the leukemic cells. Additional increases in mobility appear to be related to suppressed oxygen uptake, which results from the addition of glucose or 0.05 mM 2,4-dinitrophenol. The augmented negative surface charge does not seem to be related to those ionogenic sites susceptible to
neuraminidase
. However,
RNase
treatment of the nonleukemic tumor cell does reveal the presence in their surface membrane of negatively charged sites susceptible to this enzyme. Such
RNase
-susceptible ionogenic sites presumably redistribute at the cell surface membrane from the inner sites as a response to suppressed oxygen uptake. This results in a higher negative surface charge and increased mobility. The leukemic cells, on the other hand, did not show any change in oxygen uptake or mobility in the presence of glucose. Moreover, the reduced rate of oxygen uptake induced by the addition of 0.05 mM 2,4-dinitrophenol did not result in any significant alterations in mobility. This is consistent with the observation that the ionogenic sites susceptible to
RNase
do not appear at the surface of the leukemic cells upon suppressed oxygen uptake. The leukemic cells have thus been shown to differ from the nonleukemic tumor cells in certain aspects of their glucose metabolism as well as in the electrophoretic properties of their surface.
...
PMID:Mechanism of the linkage between te electrophoretic mobility and oxygen uptake of ascites tumor cells. 743 7
Recombinant human interferon-gamma (IFN-gamma) glycoform populations produced by Chinese hamster ovary cells have been resolved by micellar electrokinetic capillary chromatography (MECC). Separations were performed in uncoated fused silica capillaries at alkaline pH in the presence of micellar concentrations of the anionic detergent sodium dodecyl sulfate (SDS). Maximum resolution was obtained reproducibly with high-ionic-strength borate/SDS electrophoresis buffer. Under the conditions described, glycoform migration time was inversely related to the amount of carbohydrate associated with the protein. Digestion of IFN-gamma with peptide-N-glycosidase F allowed virtual real-time monitoring of glycosidase digests by capillary electrophoresis. Analysis of other digestions with either
neuraminidase
or endoglycosidase H (endo H) showed most IFN-gamma glycoforms to be sialylated and a minor proportion of glycoforms to be associated with oligomannose structures. While both bovine pancreas
ribonuclease
B and horse-radish peroxidase glycoforms were separated by this technique, proteins glycosylated at multiple sites such as bovine serum fetuin and human alpha 1-acid glycoprotein were not well resolved by MECC.
...
PMID:High-resolution separation of recombinant human interferon-gamma glycoforms by micellar electrokinetic capillary chromatography. 786 54
Simian parainfluenza virus 5 (SV5) is a prototype of the Paramyxoviridae family of nonsegmented negative-sense RNA viruses. The single-stranded RNA genomes of these viruses contain a series of tandemly linked genes separated by intergenic (IG) sequences flanked by gene-end (GE) and gene-start (GS) sequences. The viral RNA polymerase (vRNAP) complex is thought to enter the genome at its 3' end, and synthesis of mRNAs is thought to occur by a stop-start mechanism in a sequential and polar manner, with transcriptional attenuation occurring primarily at the intergenic regions. As a result, multiple nonoverlapping mRNA species are generated for each single entry of the vRNAP. To investigate the functions of GE, IG, and GS sequences in transcription, we constructed plasmids containing cDNAs of the full-length SV5 genome in which the gene junction sequences (GE, IG, and GS sequences) located between the hemagglutinin-
neuraminidase
(HN) and the polymerase (L) genes were replaced with the counterpart sequences from other gene junctions. By using reverse genetics, we recovered viable viruses from each cDNA construct, although their growth characteristics varied. Analysis of the HN and L mRNAs by quantitative
RNase
protection assay indicated that the ratios of HN to L mRNAs varied over a fourfold range. The alteration of the gene junction sequences also permitted examination of the hypothesized requirement for hexamer nucleotide position of the GS sites. The recovery of infectious viruses with transcription initiation sites that occurred at nucleotide positions 1, 2, 3, 5, and 6 of the hexamer suggest that the requirement is nonstringent.
...
PMID:Effect of inserting paramyxovirus simian virus 5 gene junctions at the HN/L gene junction: analysis of accumulation of mRNAs transcribed from rescued viable viruses. 1040 Jul 12
From saline extracts of Phytolacca esculenta (shoriku) roots, two phytomitogenes were isolated by salting out with (NH4),SO4 and chromatography on DEAE-cellulose and Sephadex G-100 columns. Both fractions were homogeneous on disc electrophoresis and on immunoelectrophoresis. One of these (Fraction E-2) was shown to be similar to pokeweed mitogen in respect to mol. wt (32,000) and amino acid composition. The other (Fraction E-3) was a protein of 18,000 mol. wt. Both fractions had similar biological activities to pokeweed mitogen in their ability to stimulate pig blood lymphocytes in vitro to incorporate tritiated thymidine, and to induce blastoid transformation. Both fractions contained an unusually large amount of cystine, i.e., 18 half-cystine residues % for Fraction E-2 and 22 residues % for Fraction E-3. Although these mitogens were resistant to deproteinizing procedures such as perchloric acid treatment and Sevag's procedure, the DNA synthesis-stimulating activity was inactivated by digestion with Pronase E and Nagarse, but resistant to trypsin, chymotrypsin, deoxyribonuclease,
ribonuclease
, lysozyme and
neuraminidase
. The activity was stable at acidic and neutral pH (4-7) but unstable at alkaline pH. The activity at pH 7.3 was stabilized by the addition of Ca2+ or Mg2+. On the addition of more than 2 mM of Ca2+, precipitation of mitogen occurred. From the above results the molecular basis of the mitogenic activity of shoriku mitogen is discussed.
...
PMID:Isolation and characterization of pokeweed mitogen-like phytomitogens from Shoriku, Phytolacca esculenta. 1999 19
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