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PubMedDate not supplied

[Isolation of a cytolytic strain of hog cholera virus from IB-RS2 cells (author's transl)].

An infectious agent, able to induce a definite cytopathic effect in pig kidney cell monolayers, was isolated from the IB-RS2 cell line. Immunofluorescence, seroneutralization and ultracentrifugation studies have permitted to identify this agent as hog cholera virus (HCV). Representative HCV-strains being devoid of pathogenicity in tissue culture, the practical and theoretical interest of such an isolation is discussed.

Animals↗
PubMed1979

Purification of hog liver isomerase. Mechanism of isomerization of 3-alkenyl and 3-alkynyl thioesters.

A hog liver enzyme that catalyzes the reversible conversion of 3-acetylenic fatty acyl thioester to (+)-2,3-dienoyl fatty acyl thioester has been purified to homogeneity. The enzyme is not inhibited by the allenic product that it generates. The same homogenous enzyme catalyzes the conversions of 3-cis- or 3-trans-acyl Coenzyme A derivatives to 2-trans-acyl-CoA derivatives. Four forms of the isomerase differing in charge (pI = 6.57, 6.83, 7.01, and 7.27) have been separated by isoelectric focusing. Ultracentrifugation and sodium dodecyl sulfate-gel electrophoresis indicate that each of these enzyme forms is dimeric and composed of two 45,000-dalton subunits. With 3-acetylenic substrates, all enzyme forms exhibit broad specificity for chain length (C6 to C12) and for the thioester moiety (N-acetylcysteamine (NAC), pantetheine, or CoA). The 3-cis and 3-trans olefinic substrates are active only in the form of their coenzyme A derivatives; their NAC thioesters inhibit competitively. Mechanistic studies favor an isomerization pathway by way of carbanion intermediates. The acetylene-allene isomerase described here and the reported crotonase-catalyzed hydration of allenic thioesters (Branchini, B.R., Miesowicz, F.M., and Bloch, K. (1977) Bioorg. Chem. 6, 49-52) may be responsible for the degradation of naturally occurring acetylenic and allenic acids.

Acyl Coenzyme A↗
PubMed1985

Characterization of hog thyroid peroxidase.

Several fundamental properties of purified hog thyroid peroxidase (A413 nm/A280 nm = 0.55) were investigated in comparison with bovine lactoperoxidase. The Mr of thyroid peroxidase was 71,000. The prosthetic group of thyroid peroxidase was identified spectrophotometrically as protoheme IX after the enzyme was hydrolyzed with Pronase. Optical spectra of oxidized and reduced thyroid peroxidases and their complexes with azide and cyanide were very similar to lactoperoxidase, except that lactoperoxidase had two reduced forms with the Soret band either at 446 or 435 nm, and thyroid peroxidase lacked a reduced form having the 446-nm band. From comparison of their pyridine hemochrome spectra, epsilon mM at 413 nm of thyroid peroxidase was estimated to be 114, being the same as that of lactoperoxidase. The cyanide inhibition for the reaction of thyroid peroxidase was competitive with hydrogen peroxide and the inhibition constant was in rough accord with the dissociation constant of its cyanide complex measured from spectrophotometric titration. Azide inhibited the reaction with an inhibition constant which was about one one-thousandth of the dissociation constant for its spectrally discernible complex. The azide inhibition was not competitive with hydrogen peroxide and decreased as the reaction proceeded. Aminotriazole inhibited the reaction strongly, and the inhibition was augmented during the reaction. These inhibition patterns of azide and aminotriazole were more or less observed in the reaction of lactoperoxidase, but not in the case of horseradish peroxidase. Characteristics of animal peroxidases are discussed.

Animals↗
PubMed1985

Coccidosis caused by Eimeria scabra in a finishing hog.

Coccidiosis caused by Eimeria scabra was diagnosed in a 60-kg finishing hog with severe diarrhea and weight loss. Fresh and fixed tissues from a farrowing to finishing operation in eastern Georgia were submitted. Examination of hematoxylin-eosin-stained sections of small intestine revealed large numbers of thick-walled oocysts and large macrogamonts. Although coccidiosis has been associated with diarrhea in baby pigs, coccidiosis as a cause of diarrhea in finishing swine is seldom reported.

Animals↗
PubMed1965

Hog cholera. V. Demonstration of the antigen in swine tissues by the fluorescent antibody technique.

The fluorescent antibody technique was employed to detect hog cholera virus in tissue sections of various organs from experimentally infected swine. The method proved to be highly sensitive and infection could be detected in these animals as early as three days after inoculation with the virus. Best results were obtained when tissues were collected from young animals in advanced disease rather than from sows or from pigs in the early febrile phase. Tonsil, spleen and lymph node were the tissues of choice and were most satisfactory when removed from freshly killed animals rather than from those that had died.

Animals↗
PubMed1965

Hog cholera IV. Detection of the virus in tissue culture preparations by the fluorescent antibody technique.

The fluorescent-antibody technique was employed for detection of hog cholera virus in tissue cultures inoculated with spleens of infected animals. As controls, cultures were also inoculated with material from normal swine and from those infected with other agents. In the first series 71 of 73 infected spleens, or 97 per cent, were detected. There were no false positive reactions among the controls. Results obtained with the second series of pigs showed that spleens collected during advanced stages of the disease were more satisfactory specimens than those collected earlier during the high temperature phase of infection. Findings with the third series of older swine indicated that their spleens were less satisfactory as a source of virus than those from young pigs. Tissues from freshly killed animals provided better specimen material than those from animals which had died.

Animals↗
PubMed1971

Studies on the bacterial floral of condemmed portions from arthritic hogs.

Studies were conducted on the bacterial floral of 122 excised joints and related iliac and inguinal lymph nodes, 118 whole hams and 42 shoulders from condemned arthritic hog carcasses. Erysipelothrix insidiosa was isolated from 15% of the joints and lymph nodes, 20% of the hams, and 33% of the shoulders. Beta-hemolytic streptococci were recovered from 12% of the joints and lymph nodes, 49% of the hams, and 54% of the shoulders. Staphylococcus aureus was found in 3% of the joints and lymph nodes, 16% of the hams and 14% of the shoulders. Gross tissue changes were not pathognomonic for any causative organism.

Animals↗
PubMedDate not supplied

Oxidation of D-thiazolidine-4-carboxylic acid by hog kidney D-aminoacid oxidase.

D-Thiazolidine-4-carboxylic acid is a good substrate for hog kidney D-aminoacid oxidase. Data are presented showing that the only oxidation product is delta 3-thiazoline-4-carboxylic acid, which does not undergo further spontaneous degradation. Thus, the oxidation of D-thiazolidine-4-carboxylic acid by D-aminoacid oxidase differs considerably from the oxidation of its L-isomer catalyzed by rat liver mitochondria which gives as final product N-formylcystine, possibly through the intermediate delta 2-thiazoline-4-carboxylic acid.

Animals↗
PubMed1979

Detection and partial purification of a natural heparin inhibitor from hog small intestine.

A natural occurring heparin inhibitor was detected and was partially purified from the mucosa of hog small intestine. The mucosa was homogenized and was extracted overnight in 0.15 M NaCl, 0.01 M imidazole, 0.001 M EDTA, pH 6.5. When the extract was made to 85% saturation in ammonium sulfate, a large quantity of heparin neutralizing activity was detected in the precipitate. Each small intestine contains approximately 35,000 units of heparin neutralizing activity. This heparin inhibitor was further purified by the procedures of zinc sulfate precipitation, ammonium sulfate fractionation, ethanol precipitaiton and heparin-sepharose chromatography. A 37 fold partial purification with 15% overall recovery was achieved to yield heparin inhibitor with specific activity of 50-65 units per mg of protein.

Animals↗
PubMed1979

[Studies on the increase of weights of lymphatic glands, of lymph and peritoneal fluid and their contents of chymotrypsin and virus in pigs suffering hog cholera (author's transl)].

Swine fever is conceived as a disorder of the enzyme systems, that are controled by serine proteases. The virus is replicated in the cells of the lymphomycoid complex, whereby the production of a chymotrypsin is induced. In swine fever the lymphatic glands and the lymph flow are increased. Fifteen normal pigs had chymotrypsin contents in the lymph of the body lymphnodes of 0,4 U/l, nine pigs suffering hog cholera 1,5 U/l. In the intestinal lymphnodes the chymotrypsin concentration was normally 2,9 U/l and in swine fever 3,5 U/l. Chymotrypsin which is present may induce the production of further chymotrypsin. Fourteen pigs suffering from swine fever showed increased peritoneal fluids (50 to 120 ml), whereby chymotrypsin was found in 5 cases. The lymphflow was assumed to be five times higher, when compared to control animals. This entails a seven-fold increase of chymotrypsin which enters the blood stream. In some cases the virus titers are higher in the lymph specimen and peritoneal fluids than in the serum. Increase of chymotrypsin concentration reduces the resistance of the virus in the lymph. Obviously the virus is spread in the body migrating with the lymph flow. However, the increasing chymotrypsin concentration seems to inactivate the virus and lymph retains its defense character. Detection of the fluorescent antigen is correlated with the evidence of the proteolytic precipitating antigen. After infection with the virus of swine vesicular disease increase of chymotrypsin is also evidenced in the lymph but to a lower degree. Therefore in swine fever the lymphnodes cause chymotrypsin formation to an extent which may explain the pathophysiological disorders in those physiological systems, that are controled by serine proteases.

Animals↗
PubMed1977

Hog cholera virus : sensitivity to hydrolytic enzymes.

The actions of trypsin and phospholipase C on th infectivity of Hog Cholera virus (HCV) were studied. Inactivation kinetics reveal a marked decrease of the infectivity of HC virus in the presence of these two agents. The particular sensitivity of this virus towards proteolytic action sheds light on certain of its behavior characteristics in the field. Virus infectivity seems to be dependent on the integrity of membrane phospholipids. No relation was observed between the rate of inactivation and the pathogenicity of the strains.

Animals↗
PubMed1977

Comparison of the immune response in serum and bucco-pharyngeal secretions following immunization by different routes with a live hog cholera virus vaccine (Thiverval strain).

The influence of vaccination route on local and systemic immune response was studied with hog cholera virus vaccine. Kinetics of antibody synthesis in serum and bucco-pharyngeal secretion was observed. Results show that, whatever the vaccination route (intranasal or intramuscular) a good systemic and local immune response were induced and pigs resisted to a virulent challenge. However the highest local immune response was obtained by intranasal vaccination with large vaccine dosage (10(7) P.F.U./pig). After a virulent challenge performed by intranasal route, no clear anamnestic immune response was detected in bucco-pharyngeal secretions.

Administration, Intranasal↗
PubMed1984

Passive transport of Rb+ by hog gastric (H+,K+)-ATPase.

Gastric vesicles enriched in (H+,K+)-ATPase were prepared from hog fundic mucosa and studied for their ability to transport K+ using 86Rb+ as tracer. In the absence of ATP, the vesicles elicited a rapid uptake of 86Rb+ (t 1/2 = 45 +/- 9 s at 30 degrees C) which accounted for both transport and binding. Transport was osmotically sensitive and was the fastest phase. It was not limited by anion permeability (C1- was equivalent to SO2-4) but rather by availability of either H+ or K+ as intravesicular countercation suggesting a Rb+-K+ or a Rb+-H+ exchange. Selectivity was K+ greater than Rb+ greater than Cs+ much greater than Na+,Li+. The capacity of vesicles which catalyzed the fast transport of K+ was 83 +/- 4% of maximal vesicular capacity of the fraction. Addition of ATP decreased both rate and extent of 86Rb+ uptake (by 62 and 43%, respectively with 1 mM ATP) with an apparent Ki of 30 microM. Such an effect was not seen on 22Na+ transport. ATP inhibition of transport did not require the presence of Mg2+, and inhibition was also produced by ADP even in the presence of myokinase inhibitor. On the other hand, 86Rb+ uptake was as strongly inhibited by 200 microM vanadate in the presence of Mg2+. Efflux studies suggested that ATP inhibition was originally due to a decrease of vesicular influx with little or no modification of efflux. Since ATP, ADP, and vanadate are known modulators of the (H+,K+)-ATPase, we propose that, in the absence of ATP, (H+,K+)-ATPase passively exchanges K+ for K+ or H+ and that ATP, ADP, and vanadate regulate this exchange.

Adenosine Triphosphatases↗
PubMed1982

Reactions of purified hog thyroid peroxidase with H2O2, tyrosine, and methylmercaptoimidazole (goitrogen) in comparison with bovine lactoperoxidase.

Stopped flow experiments were carried out with purified hog thyroid peroxidase (A413 nm/A280 nm = 0.42). It reacted with H2O2 to form Compound I with a rate constant of 7.8 X 10(6) M-1 s-1. Compound I was reduced to Compound II by endogeneous donor with a half-life of 0.36 s. Compound I was reduced by tyrosine directly to the ferric enzyme with a rate constant of 7.5 X 10(4) M-1 s-1. Tyrosine could also reduce Compound II to the ferric enzyme with a rate constant of 4.3 X 10(2) M-1 s-1. Methylmercaptoimidazole accelerated the conversion of Compound I to Compound II and reacted with Compound II to form an inactivated form, which was discernible spectrophotometrically. The reactions of thyroid peroxidase with methylmercaptoimidazole quite resembled those of lactoperoxidase, but occurred at higher speeds. The absorption spectra of thyroid peroxidase were similar to those of lactoperoxidase and intestinal peroxidase, but obviously different from those of metmyoglobin, horseradish peroxidase, and chloroperoxidase. Similarity and dissimilarity between thyroid peroxidase and lactoperoxidase are discussed.

Animals↗
PubMed1983

The immunoinhibition of hog pancreas alpha-amylase activity.

Rabbits were immunized with alpha-amylase from hog pancreas and from the antiserum the immunoglobulin fraction was separated. These immunoglobulins precipitated the enzyme and inhibited its activity. The inhibition was dependent on the amount of antibodies. It was found that an increase in the size and degree of branching of the substrate molecule (amylose, glycogen) was accompanied by an increased immunoinhibition of the enzyme. Enzyme-antibody complex was isolated on a DE-52 cellulose column and its electrophoretic mobility was different from that of the native enzyme.

Amylases↗
PubMed1981

Topology of the hog intrinsic factor receptor in the intestine.

The intrinsic factor receptor was isolated from Triton X-100 extract of hog ileal mucosa using affinity chromatography on intrinsic factor bound to cobalamin-Sepharose. We verified that the receptor contains two subunits, alpha and beta. The purified receptor located in the detergent micelle was radioiodinated. The alpha subunit was labeled and dissociated from the receptor. When the receptor was immobilized on intrinsic factor cobalamin-Sepharose, the part of the receptor which binds intrinsic factor evidently faces the gel and the rest faces outward. When such gel-bound pure receptor was iodinated, the beta subunit was labeled. Iodination of the micellar cobalamin-intrinsic factor receptor complex also caused labeling of the beta subunit. This was interpreted as being due to a conformational change in the receptor affected by the binding of the substrate cobalamin-intrinsic factor, exposing groups accessible to iodination. The beta subunit was found to be hydrophobic, but the alpha subunit was soluble in phosphate buffer without detergent. The receptor was liberated from intestinal mucosa by papain treatment. The enzyme seems to solubilize an intrinsic factor-binding part of the receptor, apparently a part of the alpha subunit. The liberated papain-alpha was purified by affinity chromatography. In gel filtration, it seemed to occur in dimeric form, but its true Mr = 45,000, according to findings in sodium dodecyl sulfate-electrophoresis. In the light of the findings, the topology of the receptor is suggested to be as follows: the alpha subunit binding intrinsic factor faces out and the hydrophobic beta subunit faces in.

Animals↗
PubMed1983

[Increase by somatocrinin of a cyclic AMP-dependent protein kinase activity in adenohypophyseal, secretory granules in the hog].

This study shows that the growth hormone hypothalamic releasing factor (somatocrinin) stimulates the activity of cyclic AMP-dependent protein kinase associated with a purified fraction of hog anterior pituitary secretory granules. Threshold, half-maximal and maximal concentrations (0.3, 35 pM and 10 nM, respectively, in the presence of 50 nM cyclic AMP) are similar to those observed for in vitro stimulation of growth hormone release by somatocrinin.

Animals↗
PubMed1983

Properties of hog cholera viruses recently isolated in Japan.

Hog cholera (HC) viruses newly isolated in Japan in 1980 and 1981 were examined for pathogenicity and serological properties by the neutralization test with antisera against bovine viral diarrhea-mucosal disease (BVD . MD) and HC viruses. Five of 23 isolates examined were neutralized poorly by BVD . MD antibody, but well by HC antibody. On the contrary, 15 isolates were neutralized readily and two isolates moderately by BVD . MD antibody. The other one reacted poorly with either HC or BVD . MD antibodies. The isolate neutralized poorly by BVD . MD antibody was more highly pathogenic than those neutralized readily. It was concluded that the antigenic properties and pathogenicity of the HC viruses were not monotype , and that HC viruses varying in antigenicity and pathogenicity were present in the field.

Animals↗