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At least 343 records · Page 19Linked to original sources
PubMed1989

Monoclonal antibody HK4001 completely inhibits K(+)-dependent ATP hydrolysis and H+ transport of hog gastric H+,K(+)-ATPase.

A monoclonal antibody (designated as HK4001) was prepared against hog gastric H+,K(+)-ATPase. It dose-dependently inhibited the H+,K(+)-ATPase activity, formation of the K(+)-sensitive phosphoenzyme, and proton uptake into gastric vesicles. The H+,K(+)-ATPase activity was completely inhibited by addition of the antibody at a molar ratio of 1:2 (antibody/catalytic subunit) at pH 7.8. The maximal inhibition decreased with decrease in pH of the medium (7.8 greater than 7.4 greater than 6.2). The Fab fragment obtained by digestion of the antibody with papain was also inhibitory. The antibody did not inhibit the K(+)-dependent p-nitrophenylphosphatase or the labeling of the enzyme with fluorescein isothiocyanate. It inhibited gastric H+,K(+)-ATPase from rabbits and rats, but did not cross-react with related cation-transport ATPases (Na+,K(+)-ATPase or Ca2(+)-ATPase) or H(+)-ATPase in the multivesicular body. From these and related findings, the antibody was suggested to recognize a highly specific site on the cytosolic surface of H+,K(+)-ATPase. The conformation of the epitope was conserved after treatment with Triton X-100, but not sodium dodecyl sulfate. In addition, judging from the stoichiometry of inactivation of H+,K(+)-ATPase by this antibody, the functional unit of H+,K(+)-ATPase was suggested to be a dimer or a tetramer (not a trimer) of the catalytic unit.

Adenosine Triphosphatases↗
PubMed1994

Indomethacin inhibition of hog gastric H+/K(+)-ATPase arises from its effect on both the enzyme protein and the lipid bilayer.

Indomethacin showed a dose-, time-, and pH-dependent, noncompetitive inhibitory effect on hog gastric H+/K(+)-ATPase. Four percent of total indomethacin in the buffer (0.20 mmol/liter) bound to the H+/K(+)-ATPase vesicles (15 micrograms/ml). It markedly quenched the intrinsic fluorescence of the enzyme, and decreased the membrane fluidity. Thus, the inhibitor effect of indomethacin may arise from both a direct effect on the hydrolytic and H+ transport functions of the enzyme and a disturbing effect on the lipid bilayer of the vesicle.

Adenosine Triphosphatases↗
PubMed1977

Association-dissociation of the flavoprotein hog kidney D-amino acid oxidase. Determination of the monomer-dimer equilibrium constant and the energetics of subunit association.

The enzyme concentration dependence of spectrophotometric titrations of hog kidney D-amino acid oxidase [EC 1.4.3.3] with p-aminobenzoate was studied. The monomer-dimer equilibrium constant of the oxidized holoenzyme at 25 degrees C was estimated to be 7 X 10(5)M-1 at pH 7.5 and 4X 10(6)M-1 at pH 8.3. The energetics of subunit association are discussed.

4-Aminobenzoic Acid↗
PubMed1977

Two forms of farnesyl pyrophosphate synthetase from hog liver.

Two forms of farnesyl pyrophosphate synthetase were separated from hog liver extracts by DEAE-Sephadex chromatography. They were designated as farnesyl pyrophosphate synthetase A and B, in order of elution. Both enzymes catalyzed the exclusive formation of E,E-farnesyl pyrophosphate from isopentenyl pyrophosphate and either dimethylallyl pyrophosphate or geranyl pyrophosphate. They also showed no detectable differences in pH optima, molecular weights, and susceptibilities to metal ions. However, the catalytic activity of the synthetase B was greatly stimulated by the addition of common sulfhydryl reagents. This stimulation was the result of conversion of the synthetase B into the synthetase A. Conversely the synthetase A was converted into form B when it was dialyzed against a buffer solution containing cupric ions. It is suggested that the formation and cleavage of disulfide bond(s) is involved in the interconversion between the two forms.

Animals↗
PubMed1978

Ca2+/protein modulator-dependent and -independent cyclic GMP phosphodiesterase from hog heart.

Ca2+/protein modulator-dependent and -independent guanosine 3':5'-monophosphate (cGMP) phosphodiesterases were separated from hog heart. The protein modulator-free Ca2+/protein modulator-dependent enzyme was partially purified by repeated DEAE-cellulose column chromatography and heat treatment. The final preparation of this enzyme showed no significant basal activity under the standard assay conditions. Lineweaver-Burk plots of the Ca2+/protein modulator-dependent enzyme activity indicated the presence of only a single kinetic form of the enzyme with Km=2.0 X 10(-6) M for for cGMP, whereas the plots for the independent enzyme were anomalous, showing both high and low K m values for cGMP. The Ca2+/protein modulator-dependent enzyme proved relatively stable at 48 degrees C for 1 h, but the independent form lost its activity under the same conditions. Furthermore, 50% inhibition of the dependent enzyme activity, but only 10% inhibition of the independent enzyme activity, was observed with 0.1 mM adenosine 3':5'-monophosphate (cAMP) when 1 muM cGMP was employed as a substrate.

3',5'-Cyclic-GMP Phosphodiesterases↗
PubMed1982

Isolation and characterization of four forms of kallikrein from hog pancreas autolysate.

Four forms of kallikrein, designated as I-IV, were isolated from hog pancreas autolysate mainly by chromatographies on Lysine-aminohexyl-Sepharose and on DEAE-Sepharose CL-6B, with yields of 65, 56, 59, and 41 mg, respectively, from 10 kg of the tissue. They were homogeneous on polyacrylamide gel electrophoresis, indistinguishable from each other immunologically and had the same amino acid composition. Kallikreins I, II, and III contained carbohydrate, but kallikrein IV was essentially carbohydrate free. On reduction with mercaptoethanol, each of them produced two polypeptide chains with different molecular weights. The H (heavy) chains from kallikreins I and II were identical, designated as H1. It was a glycoprotein with apparent molecular weight of 21,000, whereas the H chain from III and IV, designated as H2, had a molecular weight of 17,000 and was regarded as an H1 chain devoid of carbohydrate. Likewise, the L (light) chain from kallikreins I and III, designated as L1, was a glycoprotein with an apparent molecular weight of 12,000, whereas L2 from II and IV corresponded to L1 devoid of carbohydrate and had a molecular weight of 8,500. Thus, kallikreins I-IV could be expressed as H1L1, H1L2, H2L1, and H2L2, respectively. They had comparable specific activities and Km values towards synthetic substrates. The isoelectric points of kallikreins I-IV were nearly the same, with values of 4.0-4.1.

Amino Acids↗
PubMed1982

Thermodynamic characterization of hog kidney D-amino acid oxidase apoenzyme in concentrated guanidine hydrochloride solution. Preferential interaction with the solvent components and the molecular weight of the monomeric unit.

This paper describes the physical characterization of the monomeric unit of hog kidney D-amino acid oxidase apoenzyme in 6 M guanidine hydrochloride (GuHCl) solution by means of differential refractometry, densimetry, light scattering, equilibrium sedimentation, and high-speed gel filtration chromatography. In 6 M GuHCl solution, the oxidase interacts preferentially with GuHCl: the values of the preferential interaction parameter are 0.11 +/- 0.03 (S.D.) g/g of protein by densimetry and 0.14 +/- 0.04 g/g of protein by refractometry. The volume change, delta V, of the oxidase on transfer from the native to the denatured state is -350 ml/mol. The molecular weight of the monomeric apoenzyme is 39,600 +/- 1,700 by light scattering and 38,000 +/- 1,200 by high-speed equilibrium sedimentation. The values of the molecular weight estimated by the empirical methods, i.e., sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis and high-speed gel filtration chromatography in 6 M GuHCl, agree well with those obtained by the thermodynamic methods mentioned above. These results confirm definitely that the complex of the apoenzyme with SDS normally behaves in the same manner as those of standard proteins in SDS-gel electrophoresis. This is also supported in this study by the analysis of the electrophoretic data at several gel concentrations by Ferguson plots. The molecular weight of quasi-D-amino acid oxidase apoenzyme was also examined by the empirical methods.

Animals↗
PubMed1983

Orientation of thyroid peroxidase in hog thyroid microsomes.

The orientation of thyroid peroxidase in hog thyroid microsomes was studied by trypsin treatment, gel filtration, binding to Concanavalin A Sepharose and iodination of thyroglobulin. Trypsin treatment of microsomes did not solubilize the thyroid peroxidase activity completely but solubilized the NADPH-cytochrome c reductase activity almost completely. The apparent molecular size of thyroid peroxidase was not altered by trypsin treatment of microsomes. It was, however, decreased by the same treatment of deoxycholate-treated microsomes. On the other hand, the apparent molecular size of NADPH-cytochrome c reductase was reduced by trypsin without prior deoxycholate treatment. Thyroid peroxidase of microsomes did not bind to Concanavalin A Sepharose. Thyroglobulin added exogenously was not iodinated by microsomes, but endogenous thyroglobulin, which had been associated with microsomes, was iodinated. Similar results were obtained with rough microsomal membranes prepared from crude microsomes by sucrose density gradient centrifugation. These results suggest that thyroid peroxidase is oriented toward the luminal side of the microsomal vesicles.

Animals↗
PubMed1985

Characterization of a monoclonal antibody to hog thyroid peroxidase and its use for immunohistochemical localization of the peroxidase in the thyroid gland.

A monoclonal antibody (30.1.2) to hog thyroid peroxidase was produced, purified, and characterized. The IgG of 30.1.2 formed an immune complex with the peroxidase in a 1:2 or 1:1 molar ratio depending on the IgG to antigen ratio in the incubation mixture. Immune complex formation did not inhibit the peroxidase activity, which was actually activated 2-fold in the 1:1 complex. Studies of the binding of the conjugate of the IgG or its Fab' with horseradish peroxidase to untreated and acetone-treated thyroid microsomes showed that the IgG conjugate could bind to only a very small portion of the total binding sites (thyroid peroxidase) present in untreated microsomes even after prolonged incubation. The binding of the Fab' conjugate to untreated microsomes, on the other hand, increased as the incubation time was increased, reaching 40% of the total sites after 20 h of incubation. These findings indicated that thyroid peroxidase is localized on the inner surface of the microsomal membranes and that the Fab' conjugate, but not the IgG conjugate, can slowly penetrate through the membrane barrier to reach the peroxidase. Immunohistochemical experiments using the Fab' conjugate as a probe revealed that most thyroid peroxidase in the thyroid gland is located in the endoplasmic reticulum and perinuclear cisternae of the follicular cell, although a small amount could occasionally be detected in the apical membrane including microvilli. In contrast to previous reports, no thyroid peroxidase could be found in other cellular structures such as Golgi apparatus and apical vesicles by the immunohistochemical technique employed.

Animals↗
PubMed1997

Effect of processing systems on protein quality of feather meals and hog hair meals.

Experiments were conducted to evaluate the effects of five commercial processing systems and to a lesser extent, processing temperature within system, on protein quality of feather meals (FM). Two hog hair meals (HH) were also evaluated. True digestibilities of AA were determined with a 48-h excreta collection assay using cecectomized cockerels. Protein efficiency ratio (PER; grams of gain:grams of CP consumed) was determined with chicks by feeding Met-fortified 15% CP diets containing a FM or HH as the sole source of dietary protein. The six FM samples averaged 88.7% CP, 1.99% Lys, 4.83% Cys, and 0.71% Met on a DM basis. For HH, these values were 92.6, 2.78, 3.76, and 0.85%, respectively. True digestibilities of amino acids and PER of the FM varied among processing systems (e.g., lysine digestibility range was 58 to 72%, PER range was 0.71 to 1.13). Increasing the temperature during processing had no significant effect on protein quality of one FM and one HH. Digestibilities of AA in the FM water-soluble fraction collected after cooking were higher than those in the insoluble fraction. True amino acid digestibility coefficients for FM were higher than those for HH, whereas the PER of several FM were lower than those of HH. The latter response was probably due to the higher Lys content in the HH. The results of this study suggested that type of commercial processing system or conditions can affect the protein quality of FM.

Amino Acids↗
PubMed1987

A search for endogenous Na+,K+-ATPase inhibitor in acutely volume-expanded hog plasma led to lysophosphatidylcholine gamma-stearoyl.

An Na+,K+-ATPase inhibitor possessing inhibitory activity against the specific binding of ouabain to Na+,K+-ATPase has been purified from the plasma of acutely saline-infused hogs. The purification was performed by a combination of Amberlite XAD-2 adsorption chromatography and five steps of high-pressure liquid chromatography (HPLC). Fast atom bombardment mass and proton nuclear magnetic resonance (NMR) spectrometric studies identified the purified substance as lysophosphatidylcholine gamma-stearoyl (LPCS). The ouabain-displacing activity in plasma, due to this compound, increased with time during saline infusion. The maximal level reached was approximately 12 times higher than that in the pre-infusion plasma sample. Lysophosphatidylcholines (LPCs) containing myristoyl, palmitoyl and oleoyl groups were also inhibitory to Na+,K+-ATPase and ouabain-binding to the enzyme. These LPCs were effective at 100 mumol/l concentrations in attaining 50% inhibition of the enzyme activity and ouabain-binding activity of Na+,K+-ATPase. These results suggest that LPCs containing long chain fatty acids could play an important role as a Na+,K+-ATPase inhibitors under volume-expanded conditions.

Animals↗
PubMed1978

A direct plaque assay for hog cholera virus.

Direct plaque formation with representative strains of hog cholera virus (HCV) has been obtained using several pig kidney cell lines under agar overlay. HCV-infected cells appear as hazy plaques when viewed against an indirect light source, and as white plaques after neutral red staining. HCV assay by direct plaque procedure is rapid and convenient and gives infectivity titres identical to the fluorescent focus assay technique.

Cell Line↗
PubMed1989

Topographical and functional mapping of epitopes on hog cholera virus with monoclonal antibodies.

Competitive binding studies and antigen capture assays were done with monoclonal antibodies (MAbs) raised against hog cholera virus (HCV) to map the corresponding epitopes. A model was constructed in which the 13 epitopes were situated in four distinct antigenic domains: A, B, C and D. Domain A was subdivided into A1, A2 and A3. The functional relevance of this model was assessed by the characterization of pestivirus strains, by neutralization studies with the MAbs, and by isolation of variants that escaped neutralization. The topographical arrangement of the epitopes, as constructed in the model, was corroborated by the functional assays. The MAbs that defined domains A1 and A2 recognized all 94 HCV strains tested. Domains A3, B, C and D varied among the HCV strains. Neutralization was observed with MAbs defining domains A1, B and C. Synergistic neutralization occurred using MAbs against domains A1 and B, and A1 and C, but not within the domains. With MAbs defining A1, B or C, variants could be isolated that escaped neutralization and immunostaining by these MAbs.

Antibodies, Monoclonal↗
PubMed1990

Immunoaffinity purification and characterization of the envelope protein E1 of hog cholera virus.

The envelope protein E1 of hog cholera virus (HCV) was isolated by immunoaffinity purification with monoclonal antibodies (MAbs) directed against HCV. E1 consisted of a doublet of glycoproteins which varied in size from 51K to 56K between the three strains tested. E1 contains major antigenic determinants of HCV which are conserved, and are involved in neutralization by MAbs. In infected cells, E1 was found always connected with a glycoprotein of 31K. When N-linked glycans were removed, E1 had a polypeptide backbone of approximately 47K. After proteolytic cleavage of E1 with Staphylococcus protease V8 and after electrophoresis and electrotransfer, peptide fragments containing different antigenic domains of E1 were detected with MAbs directed against HCV.

Animals↗
PubMed1993

Epitope mapping of envelope glycoprotein E1 of hog cholera virus strain Brescia.

Four antigenic domains (A, B, C and D) on envelope glycoprotein E1 (gp51-54) of hog cholera virus strain Brescia have been specified by using 13 monoclonal antibodies (MAbs) that recognize non-conserved and conserved epitopes. It was shown that the non-conserved epitopes map to the N-terminal half of E1 by analysis of chimeric E1 proteins of strains Brescia and C. Conserved epitopes, however, could not be mapped using this approach. Here we describe mapping of both conserved and non-conserved epitopes on E1 by the use of an extensive set of single and double deletion mutants of E1 of strain Brescia. Deletion mutants were transiently expressed in COS1 cells and analysed by immunostaining with the 13 MAbs directed against strain Brescia and four MAbs directed against strain C. All MAbs bound to the N-terminal half of E1, i.e. amino acids 690 to 866 encoded by the sequence of strain Brescia. Domain B and one epitope in domain C are located between residues 690 and 773. Other epitopes in domain C are located on an extended region, i.e. between residues 690 and 800. Conserved epitopes of domain A are mapped between residues 766 and 866, whereas the only non-conserved epitope in this domain is located between residues 766 and 813. Domain D, represented by one MAb, is located in the same region as this non-conserved epitope of domain A, i.e. between residues 766 and 800. The results suggest the presence of two distinct antigenic units on E1, one consisting of domains B and C and the other consisting of domain A.

Amino Acid Sequence↗
PubMed1994

Virulence and pathogenesis of non-virulent and virulent strains of pseudorabies virus expressing envelope glycoprotein E1 of hog cholera virus.

Pseudorabies virus (PRV) expressing the envelope glycoprotein E1 (E1) of hog cholera virus (HCV) was used as a model to study the potential risks connected with the use of a live herpesvirus vaccine expressing a foreign gene. The gene encoding E1 was inserted into the glycoprotein X (gX) locus of both a virulent PRV strain and a non-virulent PRV strain in which the virulence genes encoding glycoprotein I (gI) and thymidine kinase (TK) had been inactivated. We investigated whether strain M205 (gI-, TK-, gX-, E1+) had a changed cell or host tropism or virulence compared with strain M206 (gI-, TK-, gX-) in pigs, rabbits, hamsters, rats, mice and rhesus monkeys. The insertion of E1 into this non-virulent PRV strain caused no change in cell or host tropism. However, pigs inoculated with M205 shed less virus over a shorter period than pigs inoculated with M206. Theoretically, virulent PRV strains expressing E1 (gX-, E1+) could arise through transfer of the E1 gene of M205 to a virulent PRV strain. Therefore, we inoculated pigs with strain M12 (gX-, E1+) or the control strain M104 (gX-) and compared the virulence and pathogenesis. M12 and M104 were of approximately equal virulence and the pathogenesis of both strains was similar. We concluded that incorporating E1 of HCV into the gX locus of PRV did not change cell or host tropism, nor did it change the virulence of either non-virulent or virulent PRV.

Animals↗
PubMed1975

Characterization of three new fucolipids from hog gastric mucosa.

Three new fucolioids have been isolated from the water-soluble glycolipid fraction of hog gastric mucosa. Fucolipid A and C exhibited blood-group-A activity, whereas Fucolipid B was not active in A-anti-A, B-anti-B and H-anti-H systems. The structures of these glycolipids were identified by partial acid hydrolysis and methylation analysis, as: (see article)

Animals↗
PubMed1976

Partial characterization of hog renin purified by affinity chromatography.

A method has been set up to purify renin on a large scale by affinity chromatography using Pepstatin, a potent inhibitor of renin, as a ligand. Pepstatin was covalently coupled to Sepharose via six different spacer 'arms'. The Sepharose-hexamethylenediamino-Pepstatin appeared to be the better derivative for renin purification even at a concentration as low as 160 nmol of Pepstatin/ml of moist gel. Renin was extracted from 100 kg of hog kidneys and semi-purified by ammonium sulfate precipitations and chromatography on DEAE-cellulose. The active fraction (48.5 g of proteins) was applied on a 500-ml affinity column. Renin was eluted in the starting buffer containing 6 M urea. Renin was purified 120-fold by the affinity chromatography step with a 79% recovery. Physico-chemical characterization of highly purified renin was performed. Isoelectrofocusing on a pH gradient from 3 to 6 showed a major peak with an isoelectric point (pI) of 4.95 and a minor peak (pI = 4.70). Polyacrylamide gel electrophoresis, pH 7.8, at different gel concentrations, showed a single peak of renin activity which was found in the major protein band. Molecular size estimated on agarose-acrylamide gel filtration was 40 000. All these physical parameters were similar before and after purification.

Animals↗