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At least 163 records · Page 9Linked to original sources
PubMed1992

Survival of hog cholera virus (HCV) in sausage meat products (Italian salami).

Survival of hog cholera virus (HCV) was determined in several sausage meat products (Italian salami) prepared with meats from experimentally infected hogs slaughtered at the peak of disease. Meats were processed following the technology applied by the main factories of the typical Italian production. The survival of HCV was assessed through inoculation in both PK 15 cell monolayers and fully susceptible piglets. In all types of sausages examined HCV was detected up to 75 days of curing by piglet inoculation. This technique was much more sensitive than use of cell culture.

Animals↗
PubMed1979

Amino terminal sequence of hog intrinsic factor.

1. Hog intrinsic factor has been purified from gastric mucosa by labile ligand affinity chromatography. 2. The following N-terminal amino acid sequence has been determined: Thr-Arg-Ser-Ser-Cys-Ser-Val-Pro-Ser-Ala-Glu-Gln-Pro-Leu-Val-Asn-Gly-Ile- Gln-Val - Leu-Met. 3. However, approx 60% of the preparation lacked the first two residues. 4. A high degree of homology between the amino terminal sequence of human and hog intrinsic factor exists.

Amino Acid Sequence↗
PubMed1989

Comparative immunology of mammalian uricase using anti-hog liver uricase.

1. Uricase was partially purified from livers of five mammals (dog, bovine, horse, house musk shrew and guinea pig), and its immunological properties were studied using anti-hog liver uricase prepared in rabbits. 2. Results obtained by immunodiffusion suggest that hog uricase has four sites of partial antigens (a, b, c, d), while the enzyme of other mammals has only part of them, and a cladogram of these six mammals is presented showing development of partial antigens. 3. Results obtained by immunoelectrophoresis suggest that the protein structure of house musk shrew uricase is considerably different from the other five mammals tested.

Animals↗
PubMed2000

Reversible and potent uncoupling of hog gastric (H(+)+K(+))-ATPase by prodigiosins.

Prodigiosin, prodigiosin 25-C, and metacycloprodigiosin all strongly inhibited the acidification activity of (H(+)+K(+))-ATPase on membrane vesicles from hog gastric mucosa (IC(50) = 32 to 103 pmol/mg protein). But, the prodigiosins, unlike omeprazole, showed little inhibitory effect on K(+)-dependent ATPase (K(+)-ATPase) activity, although at higher concentrations they inhibited K(+)-ATPase activity with an IC(50) of 1.5 to 3.0 microM. Furthermore, the inhibitory effect of the prodigiosins was rapid and completely reversible unlike that of omeprazole, and the mode of inhibition was non-competitive with respect to ATP. Hog gastric (H(+)+K(+))-ATPase itself showed an absolute requirement of halide (effectively, chloride) for acidification activity. Prodigiosins also showed a chloride requirement for inhibition of vesicular acidification, and quickly reversed the acidification of vesicular pH to neutrality even in the presence of N, N'-dicyclohexylcarbodiimide (DCCD), showing their ionophoric nature of acidification inhibitory activity. In fact, tributyltin chloride (TBT, an OH(-)/Cl(-) exchange ionophore) also inhibited vesicular acidification, but it inhibited K(+)-ATPase activity too. Finally, the prodigiosins inhibited the acid secretion from parietal cells isolated from rabbit gastric mucosa. These results suggest that prodigiosins are potent reversible uncouplers of (H(+)+K(+))-ATPase that inhibit gastric acid secretion.

Adenosine Triphosphate↗
PubMed1997

The hog intestinal mucosa acylase I: subcellular localization, isolation, kinetic studies and biological function.

The soluble acylase I (N-acylamino acid amidohydrolase, EC 3.5.1.14) from hog intestinal mucosa was 11,000-fold purified for the first time using a new four-step procedure involving an immunoaffinity chromatography. The resulting protein, which had an isoelectric point of 5.2 and a M(r) of 90,000 was composed of two apparently identical N-acylated polypeptide chains. Its amino acid composition was comparable to that of hog kidney acylase I. The enzyme had a pH optimum at 8.0 and required Zn2+ or Co2+. The optimal temperature for the acylase reaction was 40 degrees C and the activation energy of thermodenaturation was estimated at 260 kJ mol-1. The enzyme was strongly inhibited when preincubated with chelating agents, by diethyl pyrocarbonate under histidine-modifying conditions as well as by sulfhydryl compounds. The reaction of the purified enzyme with the synthetic substrate furylacryloyl-L-methionine was partly characterized as follows: Km = 0.22 +/- 0.03 mM, kcat = 128.0 +/- 17.8 s-1 and kcat/Km = 5.8 +/- 1.6 x 10(5) M-1 s-1. The L-stereoisomer of methionine competitively inhibited the enzyme reaction with a Ki of 3.4 +/- 0.2 mM. It is suggested that acylase I might not only be involved in the catabolism of intracellular N-acylated protein but also be responsible for the biological utilization of N-acylated food proteins.

Amidohydrolases↗
PubMed1999

Distribution and subcellular localization of acylpeptide hydrolase and acylase I along the hog gastro-intestinal tract.

The distribution of acylase I and acylpeptide hydrolase along the hog small intestine was investigated. No significant changes in their respective specific activity was found when the intestine was cut off and divided into eight segments (taken every 200 cm) so as to specifically study the duodenum, jejunum and ileum. Upon performing subcellular fractionation of hog enterocytes, it was observed that acylpeptide hydrolase is a soluble enzyme, while acylase I is essentially a soluble protein accounting for only 5% of the activity associated with the whole membrane fraction. The membrane-bound acylase I was neither solubilized by phosphatidylinositol-specific phospholipase C from Bacillus cereus nor by detergents which are commonly used to solubilize alkaline phosphatase, a glycosylphosphatidylinositol-anchored protein. When a phase separation was carried out in Triton X-114, all the anchored-membrane proteins of the intestinal membranes were located in the detergent-rich phase, while acylase I was present in the detergent-poor phase. Finally, the immunolabeling of intestinal cells with specific antibodies definitively established the cytoplasmic localization of acylase I. Acylpeptide hydrolase and acylase I therefore both are located in the enterocyte cytoplasm.

Amidohydrolases↗
PubMed2000

Detection of Trypanosoma evansi in brains of the naturally infected hog deer by streptavidine-biotin immunohistochemistry.

Twenty-four percent of hog deer (Cervus porcinus) that ranged free on a farm in Samut Prakarn province, Thailand, died showing nervous signs between September 1997 and February 1998. The nervous signs shown by most of them included ataxis, paresis of hind limbs, lateral recumbency, excitation and convulsion. Six animals and one carcass were submitted for diagnosis at the National Institute of Animal Health, Bangkok. Trypanosoma evansi was detected in blood and cerebrospinal fluid of four and five animals, respectively. Antibodies to T. evansi were found in all the hog deer by indirect enzyme-linked immunosorbent assay. Histopathological observation revealed a generalised non-suppurative meningoencephalitis affecting the white and grey matter at all levels of the brain. Typically, there were broad perivascular cuffs of mononuclear inflammatory cells, including lymphocytes, and some Mott cells. No trypanosomes were found in any tissue examined by conventional histopathology. However, numerous T. evansi were demonstrated by streptavidine-biotin immunohistochemistry in neuropil and Virchow-Robin spaces of brain in three animals.

Animals↗
PubMed1987

Mammalian folylpoly-gamma-glutamate synthetase. 1. Purification and general properties of the hog liver enzyme.

Folylpolyglutamate synthetase was purified 30,000-150,000-fold from hog liver. Purification required the use of protease inhibitors, and the protein was purified to homogeneity in two forms. Both forms of the enzyme were monomers of Mr 62,000 and had similar specific activities. The specific activity of the homogeneous protein was over 2000-fold higher than reported for partially purified folylpolyglutamate synthetases from other mammalian sources. Enzyme activity was absolutely dependent on the presence of a reducing agent and a monovalent cation, of which K+ was most effective. The purified enzyme catalyzed a MgATP-dependent addition of glutamate to tetrahydrofolate with the concomitant stoichiometric formation of MgADP and phosphate. Under conditions that resembled the expected substrate and enzyme concentrations in hog liver, tetrahydrofolate was metabolized to long glutamate chain length derivatives with the hexaglutamate, the major in vivo folate derivative, predominating. Enzyme activity was maximal at about pH 9.5. The high-pH optimum was primarily due to an increase in the Km value for the L-glutamate substrate at lower pH values, and the reaction proceeded effectively at physiological pH provided high levels of glutamate were supplied.

Animals↗
PubMed1987

Lysophosphatidylcholines containing polyunsaturated fatty acids were found as Na+, K+-ATPase inhibitors in acutely volume-expanded hog.

Na+, K+-ATPase inhibitors possessing inhibitory activities against the specific binding of ouabain to Na+, K+-ATPase and 86Rb uptake into hog erythrocytes have been purified from the plasma of acutely saline-infused hog. The purifications were performed by a combination of Amberlite XAD-2 adsorption chromatography and four steps of high-performance liquid chromatography with four different types of columns. Fast atom bombardment (FAB) mass and proton NMR spectrometric studies identified the purified substances as gamma-arachidoyl- [LPCA(gamma), 34%], beta-arachidoyl- [LPCA(beta), 4%], gamma-linoleoyl- (LPCL, 33%), and gamma-oleoyl- (LPCO, 25%) lysophosphatidylcholine, expressed in molar ratio in the plasma. Small amounts of gamma-docosapentaenoyl-, gamma-eicosatrienoyl-, and gamma-palmitoyllysophosphatidylcholine were also detected by both FAB mass and 1H NMR spectrometric studies. Only gamma-acyl-LPC's showed inhibitory activities on Na+,K+-ATPase and ouabain-binding activities. These LPC's were effective at 100 microM levels in attaining 50% inhibition of the enzyme activity. The inhibition of Na+,K+-ATPase activity due to these compounds was always more sensitive than that of both ouabain-binding and 86Rb uptake activities. The ouabain-displacing activity in plasma due to these compounds increased with time during saline infusion. The maximal plasma level was approximately 10 times higher than that in the preinfusion plasma sample. Although these results suggest the gamma-acyl-LPC's with long-chain polyunsaturated fatty acids are not simple competitive inhibitors to Na+, K+ -ATPase, these compounds could be implicated in the pathogenesis of the circulation abnormality through the modulation of membrane enzyme.

Animals↗
PubMed1987

alpha-Methylproline-containing renin inhibitory peptides: in vivo evaluation in an anesthetized, ganglion-blocked, hog renin infused rat model.

A structure-activity analysis of peptides containing backbone C alpha-methyl modification at the P4 site of the angiotensinogen sequence led to the discovery of potent renin inhibitors with apparent in vitro metabolic stability. Boc-alpha-MePro-Phe-His-Leu psi[CHOHCH2]Val-Ile-Amp dicitrate (Va) is a potent inhibitor of human plasma renin with an IC50 value of 1.8 nM. This peptide was shown not to be degraded in vitro by chymotrypsin, elastase, pepsin, and a rat liver homogenate preparation. It is also a potent inhibitor of hog renin with an IC50 value of 1.6 nM and was shown to elicit in vivo activity and cause dose-dependent hypotensive responses when given intravenously to anesthetized ganglion-blocked, hog renin infused rats.

Amino Acid Sequence↗
PubMed2001

An outbreak of Salmonella enteritidis infection in pygmy hogs (Sus salvanius).

An outbreak of salmonellosis was recorded in captive pygmy hogs (Sus salvanius), a critically endangered species of mammal. Of 42 captive animals maintained for conservation breeding by the Pygmy Hog Conservation Programme, Guwahati, Assam, India, 7 (16.67%) died within 3 days. The organism associated with this outbreak was identified as Salmonella enteritidis. The organisms were highly susceptible to chloramphenicol, gentamicin, norfloxacin and cefotaxim but were resistant to ampicillin, oxytetracycline, mezlocillin and sulfamerazin. The strain belonged to phage type 13a/7 and harboured two plasmids (38 and 44 megadaltons). The organisms were enterotoxigenic in CHO cell assay and were found to carry stn, sef and pef genes.

Animals↗
PubMed2000

Response of Saccharomyces cerevisiae to severe osmotic stress: evidence for a novel activation mechanism of the HOG MAP kinase pathway.

The HOG/p38 MAP kinase route is an important stress-activated signal transduction pathway that is well conserved among eukaryotes. Here, we describe a novel mechanism of activation of the HOG pathway in budding yeast. This mechanism operates upon severe osmostress conditions (1.4 M NaCl) and is independent of the Sln1p and Sho1p osmosensors. The alternative input feeds into the HOG pathway MAPKK Pbs2p and requires activation of Pbs2p by phosphorylation. We show that, upon severe osmotic shock, Hog1p nuclear accumulation and phosphorylation is delayed compared with mild stress. Moreover, both events lost their transient pattern, presumably because of the absence of negative feedback mediated by Ptp2p tyrosine phosphatase, which we found to be localized in the nucleus. Under severe osmotic stress conditions, the delayed nuclear accumulation correlates with a delay in stress-responsive gene expression. Severe osmoshock leads to a situation in which active and nuclear-localized Hog1p is transiently unable to induce transcription of osmotic stress-responsive genes. It also appeared from our studies that the Sho1p osmosensor is less active under severe osmotic stress conditions, whereas the Sln1p/Ypd1p/Ssk1p sensor and signal transducer functions normally under these circumstances.

Blotting, Western↗
PubMed2001

The Saccharomyces cerevisiae Sko1p transcription factor mediates HOG pathway-dependent osmotic regulation of a set of genes encoding enzymes implicated in protection from oxidative damage.

A major part of the transcriptional response of yeast cells to osmotic shock is controlled by the HOG pathway and several downstream transcription factors. Sko1p is a repressor that mediates HOG pathway-dependent regulation by binding to CRE sites in target promoters. Here, we report five target genes of Hog1p-Sko1p: GRE2, AHP1, SFA1, GLR1 and YML131w. The two CREs in the GRE2 promoter function as activating sequences and, hence, bind (an) activator protein(s). However, the two other yeast CRE-binding proteins, Aca1p and Aca2p, are not involved in regulation of the GRE2 promoter under osmotic stress. In the absence of the co-repressor complex Tup1p-Ssn6p/Cyc8p, which is recruited by Sko1p, stimulation by osmotic stress is still observed. These data indicate that Sko1p is not only required for repression, but also involved in induction upon osmotic shock. All five Sko1p targets encode oxidoreductases with demonstrated or predicted roles in repair of oxidative damage. Altered basal expression levels of these genes in hog1Delta and sko1Delta mutants may explain the oxidative stress phenotypes of these mutants. All five Sko1p target genes are induced by oxidative stress, and induction involves Yap1p. Although Sko1p and Yap1p appear to mediate osmotic and oxidative stress responses independently, Sko1p may affect Yap1p promoter access or activity. The five Sko1p target genes described here are suitable models for studying the interplay between osmotic and oxidative responses at the molecular and physiological levels.

Activating Transcription Factors↗
PubMed1998

Purification and characterization of a Ca2+/calmodulin-dependent protein kinase II from hog gastric mucosa using a protein-protein affinity chromatographic technique.

A peripheral member of the Ca2+/calmodulin-dependent protein kinase II (CaMkinase II) group has been purified from hog gastric mucosa with the use of a novel affinity-chromatographic step. For the well known neural isotypes of CaMkinase II, it is proposed that the subunits form holoenzymes through a specific domain at the C-terminus called the 'association domain'. We immobilized a bacterially expressed association domain from CaMkinase II-delta-2 and used it as an affinity column. This matrix was used as the last step in a sequential enzyme purification procedure from hog gastric mucosa and yielded a homogeneous CaMkinase II which showed the typical physical and enzymatic properties of CaMkinase II. The enzyme activity showed a dependence on Ca2+ and calmodulin (apparent K0.5 = 2.7 microM and K0.5 = 0.02 microM, respectively). We found a subunit molecular mass of 61 kDa. An apparent native molecular mass of 310 kDa was calculated. The Stokes radius and the sedimentation coefficient were 6.7 nm and 11.2 S, respectively. Moreover, the isolated CaMkinase II was very well inhibited by the CaMkinase-II-specific inhibitors KN-62 (Ki = 0.52 nM) and KT5926 (Ki = 0.79 nM). The phosphorylation of several substrates revealed its multifunctionality. The purified CaMkinase II had an apparent Km for Mg-ATP of 24.0 microM and for autocamtide-II of 0.62 microM. CaMkinase II is considered as a strong candidate for regulating vesicle released quanta such as acid, neurotransmitters or insulin.

1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine↗
PubMed1999

Immunohistochemical detection of hog cholera virus antigen in paraffin wax-embedded tissues from naturally infected pigs.

In 17 pigs submitted for diagnosis in 1980, hog cholera was confirmed by viral isolation, by a direct immunofluorescent antibody test for viral antigen, and by the presence of characteristic histopathological lesions. In the present study, hog cholera viral antigen was demonstrated in these pigs by immunohistochemical examination of formalin-fixed paraffin wax-embedded tissues that had been stored for 18 years. Viral antigen was detected in crypt epithelial cells of the tonsil, collecting tubular epithelial cells of the kidney, bronchial and bronchiolar mucosal and gland cells of the lung, and pancreatic epithelial cells.

Animals↗
PubMed1978

Large scale preparation of pure hog kidney renin.

The complete purification of renin raises difficult problems due to its extremely low concentration in kidney (less than 1/50,000 of total proteins). The complete purification of hog kidney renin has been realized on a large scale, starting from 300 kg of fresh hog kidneys. 14.6 mg of pure renin were obtained with an overall yield of 4%. The purification procedure involved 14 steps. The enzyme was extracted at pH 3.5. Subsequent purification steps were performed in the presence of protease inhibitors to decrease renin proteolysis. These steps included an ammonium sulfate precipitation and a batch-chromatography on DEAE-cellulose. The major purification step was an affinity chromatography on Sepharose-hexamethylene-diaminopepstatin. The enzyme obtained was further purified by molecular sieving gel filtration and isoelectric focusing.

Animals↗
PubMed1998

The high osmolarity glycerol response (HOG) MAP kinase pathway controls localization of a yeast golgi glycosyltransferase.

The yeast alpha-1,3-mannosyltransferase (Mnn1p) is localized to the Golgi by independent transmembrane and lumenal domain signals. The lumenal domain is localized to the Golgi complex when expressed as a soluble form (Mnn1-s) by exchange of its transmembrane domain for a cleavable signal sequence (Graham, T. R., and V. A. Krasnov. 1995. Mol. Biol. Cell. 6:809-824). Mutants that failed to retain the lumenal domain in the Golgi complex, called lumenal domain retention (ldr) mutants, were isolated by screening mutagenized yeast colonies for those that secreted Mnn1-s. Two genes were identified by this screen, HOG1, a gene encoding a mitogen-activated protein kinase (MAPK) that functions in the high osmolarity glycerol (HOG) pathway, and LDR1. We have found that basal signaling through the HOG pathway is required to localize Mnn1-s to the Golgi in standard osmotic conditions. Mutations in HOG1 and LDR1 also perturb localization of intact Mnn1p, resulting in its loss from early Golgi compartments and a concomitant increase of Mnn1p in later Golgi compartments.

Calcium-Calmodulin-Dependent Protein Kinases↗
PubMed1976

Brucella suis infection in Philadelphia. A survey of hog fever and asymptomatic brucellosis.

Examination of hospital and public health records revealed 19 cases of brucellosis diagnosed in Philadelphia between 1968 and 1972. A serologic survey at Philadelphia's largest hog-processing plant, however, indicated infection in 39% of workers. If extrapolated industry-wide, the total would be several hundred in Philadelphia. The infection is usually unrecognized or asymptomatic, since men were active in physically demanding jobs with agglutinin titers in excess of 1:5000. Overt illness, usually first diagnosed after weeks of incapacity, responded readily to tetracycline therapy. Although clinical manifestations are nonspecific, attention to occupational history should quickly lead to the diagnosis. It is emphasized that any hog-processing plant, wherever located, is potentially a reservoir of brucellosis. Prolonged morbidity and loss of production time might be avoided if physicians were more alert to this infection. Agglutinins in possibly significant titers were also found in a small fraction of persons without identifiable exposure.

Adult↗