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At least 235 records · Page 13Linked to original sources
PubMed1990

Identification of conserved epitopes on a hog cholera virus protein.

Eight monoclonal antibodies directed against the hog cholera virus (HCV) strain Alfort/187 and displaying broad cross-reactivity with other HCV strains were characterized. An enzyme immunoassay on fixed monolayers of porcine or bovine cells infected with 14 different strains and isolates of HCV and 12 bovine viral diarrhea viruses (BVDV), respectively, showed that all antibodies reacted with HCV only. Seven antibodies recognized all HCV tested, thus indicating that they were directed against conserved epitopes. All antibodies neutralized the homologous strain and different patterns of the other HCV tested. Radioimmunoprecipitation analysis showed that the monoclonal antibodies were directed against a doublet of 56-60 kDa, presumably representing the major envelope glycoprotein of HCV. The results of reciprocal antibody blocking assays allowed the mapping of two distinct conserved antigenic domains on this protein.

Animals↗
PubMed1989

High titre Hog Cholera virus production on Cytodex 3 microcarrier cultures.

In an attempt to produce Hog Cholera virus (HCV) preparations of high titre, optimal growth and trypsinization conditions of PK-15 microcarrier cell cultures were defined. Infecting a PK-15 Cytodex 3 microcarrier culture with HCV increased the yield of virus more than 10 times compared with conventional monolayer culture in Roux flasks.

Animals↗
PubMed1977

Improved method for the purification of hog cholera virus grown in tissue culture.

A method for purification of Hog Cholera Virus (HCV) is presented. Cell-associated virus was extracted from PK15 cells 17 hours p.i. by fluorocarbon treatment. The virus was concentrated by polyethylene glycol precipitation and partially purified by pelleting on a fluorocarbon cushion. Final purification was achieved by rate zonal centrifugation in a 7--35 per cent sucrose gradient. This procedure permits a recovery of approximately 40 per cent of viral infectivity. A specific infectivity of about 2 X 10(7) PFU/microgram of protein was achieved. An apparent density d=1.13 g/ml in sucrose and a Sw20 value of about 150 was determined for purified HC virions.

Animals↗
PubMed1995

Comparison of the entire nucleotide and deduced amino acid sequences of the attenuated hog cholera vaccine strain GPE- and the wild-type parental strain ALD.

We have determined the complete nucleotide sequences of a live attenuated hog cholera virus (HCV) and its progenitor strain. The viral RNA of each strain consisted of 12,298 nucleotides including untranslated regions of 373 and 228 bases at the 5' and 3' end, respectively. There was a single large open reading frame spanning 11,697 nucleotides which could encode a large protein of 3,899 amino acids with a calculated molecular weight of 438-kDa. We have found 225 nucleotide difference between the two strains, of which six were located in the untranslated region. Four-sixths of these differences resulted in amino acid substitutions.

Amino Acid Sequence↗
PubMed1993

Characterization of structural and non-structural proteins of hog cholera virus by means of monoclonal antibodies.

A panel of 15 monoclonal antibodies, produced against the hog cholera virus, were characterized by radioimmunoprecipitation assays. Using this panel, we were able to identify 4 sets of monoclonal antibodies precipitating each a different viral protein with relative molecular weight of 40, 46, 120 kDa, respectively, and a protein complex containing 15, 16, 27, and 55 kDa polypeptides which were further characterized. One monoclonal antibody recognized an antigenic determinant at the C-terminal cleavage product of the non-structural p 125 of BVDV. The 40 kDa protein was precipitated from the pelleted virions, indicating its structural importance. On the contrary the 46 kDa protein could only be precipitated from the cell lysate and not from the pelleted virions. The glycosylated 15/16 kDa-55 kDa proteins form a disulfide linked heterodimer on the virus particle with a relative molecular weight of 65 kDa.

Animals↗
PubMed1988

Effects of NC-1300-B, a new benzimidazole derivative, on hog gastric H+, K+-ATPase, gastric acid secretion and HCl.ethanol-induced gastric lesions in rats.

This study was designed to determine the effect of a newly synthesized benzimidazole derivative NC-1300-B on H+, K+-ATPase (proton pump) in the hog gastric mucosa and on the basal gastric acid secretion and necrotizing agent-induced gastric lesions in rats. NC-1300-B inhibited the proton pump in a concentration-dependent manner and concentrations which inhibited the enzyme activity by 50% were 4.4 x 10(-6) M at pH 6.0 and 3.1 x 10(-5) M at pH 7.4. NC-1300-B administered orally or intraperitoneally 0.5 hr before ligating the pylorus inhibited the gastric acid secretion in a dose-dependent manner. The ED50 values (doses which inhibit acid output or lesion formation by 50%) for acid secretion were 11.5 and 11.0 mg/kg with oral and intraperitoneal administration, respectively. The antisecretory effect in a dose of 100 mg/kg persisted for up to 72 hr. NC-1300-B administered orally or intraperitoneally 0.5 hr before HCl.ethanol administration protected against damage of the gastric mucosa in a dose-dependent manner. The ED50 values for lesion formation were 13.3 and 23.0 mg/kg with oral and intraperitoneal administration, respectively. This protection with an oral dose of 100 mg/kg persisted for up to 72 hr. While pretreatment with 5 mg/kg of indomethacin given subcutaneously did not appreciably reverse the NC-1300-B protection, the pretreatment with 10 mg/kg of N-ethylmaleimide given subcutaneously potently reversed the NC-1300-B protection. NC-1300-B administered intragastrically at 30 mg/kg significantly inhibited the amplitude of gastric contraction for 50 min after intragastric administration. These effects of NC-1300-B on gastric secretion and lesion formation are much the same as those of the established proton pump inhibitor omeprazole, except for the short duration of the action of omeprazole (less than 24 hr).

Adenosine Triphosphatases↗
PubMed1995

Characterization of the hog cholera virus 5' terminus.

Hog cholera virus (HoCV) 5' terminus of the ALD and GPE(-) strains were analyzed by using rapid amplification of cDNA end method (5'RACE). An additional nine nucleotides were found at the 5' termini of genomic RNA in the ALD and GPE(-) strains of HoCV. These nine nucleotides were also conserved in BVDV and were suggested to form a hairpin structure at the 5' terminus by computer-assisted analysis. It seems possible that the secondary structure and/or the 5' terminus sequence has a significant role in the HoCV virus genome.

Animals↗
PubMed1978

Effect of calcium on the H+/K+ ATPase of hog gastric microsomes.

The K+-stimulated, ouabain-insensitive ATPase activity present in vesicles of microsomal fractions from hog gastric mucosa can be demonstrated in fresh preparations by adding Ca2+ (micron range) to the incubation medium. Ca2+ effect is similar but not additive to the effect of gramicidin or freezing. High Ca2+ concentrations (1 mM) produce an inhibitory effect on the K+-stimulated ATPase activity. This effect is not seen in the presence of gramicidin. Calcium increases the magnitude of ATP-driven H+ uptake in vesicles exposed to K+ for periods of time up to 60 min. At longer times of exposure (120 min) the response does not differ from controls. It is concluded that Ca2+ at low concentrations (micron range) enhances the K+ permeability of the vesicular membrane. At higher concentrations (mM range), Ca2+ becomes inhibitory to the K+ permeability. A role for Ca2+ as a second messenger in stimulus-secretion coupling in the parietal cell is discussed.

Animals↗
PubMed1988

Characteristics of the porcine kidney cell line IB-RS-2 clone D10 (IB-RS-2 D10) which is free of hog cholera virus.

A Brazilian stock of clone C17 of the IB-RS-2 porcine kidney cell line which was contaminated with hog cholera virus (HCV) was cloned. One clone designated IB-RS-2 D10 was determined to be free of HCV, 20 other viruses, and Mycoplasma. IB-RS-2 D10 cells possessed the same viral susceptibility pattern as the contaminated parent cells to the viruses of foot-and-mouth disease, swine vesicular disease, vesicular exanthema of swine, transmissible gastroenteritis, and several other viruses. The IB-RS-2 D10 cells had a median chromosome count of 34, were morphologically epithelioid cells, and were resistant to HCV infection. Freedom from HCV affords advantages for vaccine production and avoids laboratory contamination.

Animals↗
PubMed1984

Complete purification of arginyl-tRNA:protein arginyltransferase from hog kidney and production of its antibody.

Arginyltransferase was purified 60,000-fold from the 105,000g supernatant of hog kidney by fractionation with ammonium sulfate, precipitation at pH 5.2, and chromatographies on DEAE-cellulose and hydroxyapatite, as well as affinity chromatographies on heparin-Sepharose and angiotensin II-Sepharose. Purified transferase had a specific activity of 7.6 mumol/min/mg, which was 66 times higher than that attained thus far (R. L. Soffer, 1970, J. Biol. Chem. 245, 731-737). Electrophoresis of purified transferase on polyacrylamide gel showed a single band which corresponded to the region of activity in homogenized slices of a duplicate gel. The homogeneity was also observed by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate, where only a single band of Mr 35,000 was observed, even after staining by the silver method (B. R. Oakley, D. R. Kirsch, and N. R. Morris, 1980, Anal. Biochem. 105, 361-363). Antibody to the purified transferase was prepared in a rabbit. The antibody inhibited arginyltransferase activity, and showed a single precipitin line by double immunodiffusion with crude transferase preparation.

Acyltransferases↗
PubMed1987

Properties of the lectin from the hog peanut (Amphicarpaea bracteata).

An N-acetyl-D-galactosamine-specific lectin has been isolated from the two seed forms of the hog peanut (Amphicarpaea bracteata) using an affinity support containing the synthetic type A blood group trisaccharide alpha-D-GalNAc-(1,3)-[alpha-L-Fuc-(1,2)]-beta-D-Gal (Synsorb A). The affinity-purified lectin appears to be identical in both seed types. Gel filtration on Sephadex G-200 gives a single symmetrical peak corresponding to Mr 135,000. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis shows four subunit forms, each of which contains carbohydrate. Limited amino terminal sequencing indicates heterogeneity in two of the first 10 residues. The lectin contains no cysteine. There are four equivalent, noninteracting GalNAc binding sites per 135,000-Da molecule, having an association constant for methyl N-acetyl-alpha-D-galactosaminide of 4.0 X 10(4) M-1. Precipitin and hapten inhibition studies show the lectin to be specific for terminal, nonreducing D-GalNAc units, with a preference for the alpha-anomer and enhanced specificity for the disaccharide, GalNAc alpha 1,3GalNAc. There is also a single adenine binding site per Mr 135,000 lectin molecule with an association constant of 1.3 X 10(6) M-1.

Adenine↗
PubMed1979

The use of octyl beta-D-glucoside as detergent for hog kidney brush border membrane.

Octyl beta-D-glucoside was synthetized from alpha-acetobromoglucose with an improved method yielding a very pure product with a sharp melting point (108-109 degrees C) and free of intermediate products as judged by IR and NMR spectra. The yield of the synthesis is 66% when referred to alpha-acetobromoglucose. The potency of this compound as a detergent on hog kidney brush border membranes was compared to the action of Triton X-100. Octyl glucoside preferentially extracts aminopeptidase M and gamma-glutamyltranspeptidase in a concentration-dependent manner. The more deeply imbedded membrane enzyme, alkaline phosphatase, was relatively resistent to the action of octyl glucoside. In contrast, Triton X-100 extracted all membrane proteins to about the same extent. Additionally it was found that octyl glucoside can be removed from membrane extracts by Biobead SM 2. The capacity of the beads is about 170 mg detergent/g of dry Biobead SM 2. Thus octyl glucoside seems to be a useful tool for solubilization and purification of brush border membranes proteins.

Animals↗
PubMed1981

Partial purification of hog kidney sodium-D-glucose cotransport system by affinity chromatography on a phlorizin polymer.

A brush border membrane fraction isolated from hog kidney cortex was solubilized with 0.5% Triton X-100 and subjected to affinity chromatography on a phlorizin polymer. As demonstrated by transport studies with reconstituted proteoliposomes, the polymer adsorbs the sodium-dependent D-glucose transport system. The latter can be eluted from the polymer by 0.5 M D-glucose. The purified fraction contains 0.4% of the membrane protein extract and exhibits a 20--30-fold higher transport activity than the crude membrane extract. Other brush border membrane proteins such as alkaline phosphatase and aminopeptidase M are markedly reduced in the purified fraction. Thus, affinity chromatography on a phlorizin polymer is a suitable tool for the isolation of the sodium-glucose transport system present in brush border membranes.

Animals↗
PubMed1986

Thiophosphorylation of hog gastric (H+ + K+)-ATPase membranes by endogenous protein kinases.

(H+ + K+)-ATPase-enriched membranes from hog stomachs were tested for their capacity to autophosphorylate using [gamma-32P]ATP or [gamma-35S]ATP[S] as phosphate donors. The radioactive polypeptides were characterized by SDS-PAGE. In the presence of Mg2+ and 5 microM [gamma-32P]ATP, rapid and transient incorporation of 32P occurred at 0 degrees C. Radioactivity was essentially found in the major polypeptide of the material, the 95 kDa subunit of (H+ + K+)-ATPase. Under the same experimental conditions, thiophosphorylation was slower and reached a plateau within 1 h. Incorporation levels were higher with manganese than with magnesium. After one hour at 0 degrees C, and in the presence of 10 mM manganese and 5 microM ATP[S], 0.58 +/- 0.06 nmoles of thiophosphate were incorporated per mg of protein. Twenty seven percent of the thiophosphorylated amino acids were acylphosphates i.e. likely to be the ATPase thiophosphointermediate. The remaining thiophosphorylated amino acids (73%) were thought to be produced by protein kinases. This was supported by the autoradiographies of membrane SDS-PAGE which indicated that, in addition to the 95 kDa ATPase subunit, other polypeptides were thiophosphorylated especially at 108, 58, 47, 45 and 36-40 kDa. A previous study had provided strong evidence that chloride transport in gastric microsomes, is modulated by a protein kinase-dependent phosphorylation (Soumarmon, A., Abastado, M., Bonfils, S. and Lewin M.J.M. (1980) J. Biol. Chem. 255, 11682-11687). In the present work, we demonstrate that the peptidic inhibitor of cAMP-dependent protein kinases decreased thiophosphorylation of a 45 kDa polypeptide. We suggest that this polypeptide could be regarded as a candidate for the role of chloride transporter or chloride transport regulator.

Animals↗
PubMed1975

Intracellular distribution of beta-galactosidases in mucosal cells from hog small intestine.

1. Intracellular distribution of three types of beta-galactosidases (beta-D-galactoside galactohydrolase EC 3.2.1.12) i.e. hetero beta-galactosidase, lactase and acid beta-galactosidase, was studied by examining the properties of subcellular fractions isolated by a systematic fractionation of mucosal cells of the small intestine of the hog. Localization of hetero beta-galactosidase in cytosol could be shown. 2. Localization of lactase in the brush borders was shown by analyzing the purified brush borders prepared separately. 3. To domonstrate the lysosomal localization of acid belta-galactosidase, lysosomes were purified separately and their extract was chromatographed on a hydroxylapatite column. The activities of various enzymes in the purified lysosomes as well as in the intermediary fractions obtained during lysosome purification and the pattern of the hydroxylapatite chromatography led us to conclude that acid beta-galactosidase is a lysosomal enzyme.

Animals↗
PubMed1976

Chemical modifications of the crystalline quinolinate phosphoribosyltransferase from hog liver.

Amino acid analysis and chemical modification of the crystalline quinolinate phosphoribosyltransferase (EC 2.4.2.19) from hog liver were performed. The enzyme contained 29 residues of half cystine per mol. The enzyme activity was strongly inhibited by sulfhydryl reagents. The number of reactive (exposed) sulfhydryl group was determined to be 10.2 and total sulfhydryl group was to be 25.2 per mol by using 5,5'-dithiobis(2-nitrobenzoic acid). The enzyme activity was also inhibited by lysine residue-, histidine residue-, and arginine residue-modifying reagents. These results and the effect of preincubation with the substrates on chemical modifications suggest that the lysine residue, histidine residue and sulfhydryl group may be closely related to the binding site of quinolinic acid.

Amino Acids↗
PubMed1975

Blood group A active difucosyl glycolipid from hog gastric mucosa.

A new difucosyl glycolipid exhibiting blood group A activity was isolated from water-soluble glycolipid fraction of hog gastric mucosa. The structure of this glycolipid was identified by partial acid hydrolysis, sequential degradation with specific glycosidases and methylation analysis, as: "see article".

ABO Blood-Group System↗