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PubMed1983

Localization of leucine aminopeptidase in normal hog lens by immunofluorescence and activity assays.

Rabbit antisera to purified bovine lens leucine aminopeptidase (EC 3.4.11.1, LAP) were prepared and shown to be specific for leucine aminopeptidase alone (Taylor et al Cur Eye Res 2:47-56, 1982). When whole hog lens thin sections were treated first with these antisera and then with fluorescein conjugated goat anti-rabbit gamma globulin, greatest fluorescence was observed in the elongating epithelium and outer cortex, and significantly less fluorescence was observed in the lens core. That largest amounts of LAP are present in the epithelium is supported by activity measurements using leucylamide as substrate. The specific activity of LAP in the epithelium/outer cortex is 83 times that of LAP in the inner cortex. The concentration of posttranslationally (postsynthetically) modified and oxidized crystallins is greatest in the core, yet in this zone there is a paucity of aminopeptidase activity, possibly due to age-related degradation of the enzyme. It is possible that LAP is in association with membranes and present in nucleoplasm of rapidly metabolizing, elongating epithelial cells. These observations are discussed in relation to the possible role of proteolysis in cataractogenesis.

Absorption↗
PubMed1980

Persistent hog cholera infection detected during virulence typing of 135 field isolates.

During the hog cholera (HC) eradication program in the United States, 135 field isolates were characterized by inoculation into specific-pathogen-free pigs. This gave origin to the classification of 61 (45%) as high virulent, 37 (27%) as low virulent, 29 (22%) as avirulent or immunizing, and 8 (6%) as capable of causing persistent infection. The persistent infections caused by the eight isolates were of long durtion, lasting in one instance to 152 days. The persistently infected pigs remained relatively free of clinical signs of HC but had high concentrations of HC virus (HCV) in their blood. When 6 of these pigs were given a second inoculation (with the virulent Ames strain of HCV), 2 died while the health status of 4 remained unchanged.

Animals↗
PubMed1984

Biosynthesis of blood group I antigens. Identification of a UDP-GlcNAc:GlcNAc beta 1-3Gal(-R) beta 1-6(GlcNAc to Gal) N-acetylglucosaminyltransferase in hog gastric mucosa.

A beta 1-6N-acetylglucosaminyltransferase has been identified in microsomal preparations from hog gastric mucosa which is able to synthesize branch points in branched lactosaminoglycans (blood group I antigenic structures). The enzyme can be assayed specifically using the synthetic trisaccharide GlcNAc beta 1-3Gal beta 1-4Glc beta-OMe as acceptor. The product of the transferase reaction was isolated and identified by methylation analysis as, (Formula: see text) Into this tetrasaccharide two galactose residues were incorporated by the specific beta-N-acetylglucosaminide beta 1-4-galactosyltransferase from bovine milk. Thus a hexasaccharide was formed which was shown to inhibit strongly a murine monoclonal and a human anti-I antibody. Using a variety of oligosaccharides and glycolipids, which correspond to structures found in linear lactosaminoglycan chains, the acceptor substrate specificity of the branching enzyme was determined. From these results it is concluded that branching occurs only during the elongation process at the nonreducing end and follows a well-defined order. N-Acetylglucosamine is first transferred to position 3 of a terminal galactose followed immediately by the addition of a second N-acetylglucosamine to position 6; only then the 1-3 and the 1-6 branches are further elongated by galactose residues.

Animals↗
PubMed1978

Isolation and characterization of the sulfated neolactotetraosylceramide from hog gastric mucosa.

A sulfated neolactotetraosylceramide has been isolated from the lipid extract of hog gastric mucosa. Isolation procedure involved extraction of lipids with 0.4 M sodium acetate in methanol/chloroform/water, alkaline methanolysis, column fractionation on DEAE-Sephadex, separation of the acetylated acidic glycolipids on silicic acid column, and thin layer chromatography. By partial acid hydrolysis, sequential hydrolysis with specific glycosidases, periodate oxidation, and methylation analysis of the native and desulfated compound, the structure of this glycolipid is proposed to be: Galbeta1 leads to 4GlcNAc(6 comes from SO3)beta1 leads to 3Galbeta1 leads to 4Glc1 leads to 1 ceramide.

Animals↗
PubMed1983

Relaxation and Ca-spike suppression in circular and longitudinal muscles of hog bile duct ampulla by CCK-C-terminal peptides.

The mechanisms by which cholecystokinin (CCK)-C-terminal peptides relax biliary smooth muscles were investigated using circular and longitudinal muscles of hog bile duct ampulla. In normal Tyrode's solution the concentration-contraction curves for acetylcholine (ACh) were in a higher range in circular muscle than in longitudinal muscle. In K+-depolarized muscles the concentration-contraction curves for Ca2+ were in a lower range in circular than in longitudinal muscle. When the Ca2+ concentration in Tyrode's solution was decreased, circular muscle showed concentration-dependent relaxation of normal tone from 1.8 mM to zero calcium, but longitudinal muscle did not show any relaxation. Concentrations of CCK-4, CCK-6 and CCK-7 producing 50% relaxation of normal tone in circular muscles were 19 microM, and 53 nM, respectively; concentrations producing 50% inhibition of ACh-induced contraction in longitudinal muscle were 20, 13 and 47 microM, respectively. The effects of calcium removal on the membrane potential were hyperpolarization in circular muscle but depolarization in longitudinal muscle, although there was cessation of calcium spikes in both muscles. In longitudinal muscle, CCK-4 suppressed spontaneous spikes and evoked spikes. In circular muscle, CCK-4 did not suppress evoked spikes even in a concentration that caused relaxation and hyperpolarization of the membrane. In conclusion, CCK-C-terminal peptides may induce relaxation of circular muscle, not by direct suppression of calcium influx during the action potential, but by intracellular decrease in Ca2+ levels probably arising from increased calcium uptake into the sarcoplasmic reticulum or the plasma membrane. On the other hand, the peptides do not induce relaxation of longitudinal muscle, but suppress only the calcium influx (resulting in cessation of spontaneous contraction). Therefore, CCK-4 may cause a relaxation of normal tone in circular muscle, and an inhibition in the spontaneous contraction, induced by some transmitters, of longitudinal muscle.

Acetylcholine↗
PubMed1981

Purification and characterization of endo-beta-galactosidase from Escherichia freundii induced by hog gastric mucin.

A new procedure for inducing and purifying endo-beta-galactosidase from Escherichia freundii was described. The enzyme was found to be induced with high efficiency in culture medium containing Smith-degraded hog gastric mucin, which was prepared from a commercially available starting material. Endo-beta-galactosidase was then purified by ammonium sulfate fractionation, DEAE-Sephadex chromatography, and affinity chromatography on Sepharose conjugated with the Smith-degraded mucin. The enzyme thus purified by only three steps showed no other glycosidase or protease activities and had higher specific activity compared to the previous method. This new method has a great advantage since the gastric mucin is abundantly available and the efficiency of enzyme production was high without significant induction of exoglycosidase. The hydrolysis of oligosaccharides, glycosphingolipid, and keratansulfate was studied by using this newly purified enzyme. Kinetic data indicate that hydrolyzability of these substrates is largely affected by substrate concentration, enzyme concentration and the structure of substrates. Based on these results, the specificity of E. freundii endo-beta-galactosidase was discussed.

Animals↗
PubMed1983

Gangliosides of hog skeletal muscle.

The ganglioside content of hog skeletal muscle was 27 nmol/g wet weight when calculated as lipid-bound sialic acid. The elution profile on DEAE-Sephadex A-25 column chromatography showed that the monosialoganglioside fraction (61% of total lipid-bound sialic acid) contained at least seven major gangliosides and that the disialoganglioside fraction (25%) contained four major ones. These gangliosides were purified by latrobeads column chromatography, and from the results of sugar analysis, specific enzymatic hydrolysis, a permethylation study and CrO3 oxidation, the structures of these gangliosides were determined to be as follows: A, GM3(NeuAc); B, GM3(NeuGc); C, sialosylparagloboside(NeuAc); D sialosylparagloboside (NeuGc); E, GM1(NeuAc); F, GM1(NeuGc); G, sialosyllactosaminylparagloboside(NeuAc) (monosialogangliosides) and H, GD1a(NeuAc, NeuAc); I, GD1a(NeuAc, NeuGc); J, GD1a(NeuGc, NeuGc); K, GD1b(NeuAc, NeuAc) (disialogangliosides), where NeuAc is N-acetylneuraminic acid and NeuGc is N-glycolylneuraminic acid as sialyl groups. The major fatty acids of gangliosides A, D and G were mainly C16:0, but those of the others, E, F, H, J and K, were C16:0, C18:0, C22:0 and C24:0. The long-chain bases were predominantly C18:1 sphingosine in all gangliosides.

Animals↗
PubMed1981

Totally inactive renin zymogen and different forms of active renin in hog brain tissues.

The nature of the activable form of renin in the kidney and other tissues has not been clear. Its identification and isolation from kidney have been hampered by rapid activation due to high levels of proteases. Using a pepstatin-Sepharose column, which distinguishes inactive renin from the active enzyme, evidence was obtained for the presence of a totally inactive zymogenic precursor of renin in the pituitary, pineal, and other regions of hog brain. The precursor has an approximate molecular weight of 50,000 and conversion to the active enzyme causes reduction in molecular weight to 43,000. Conversion of this active enzyme to an active but high molecular weight form (60,000) was also observed when the pituitary extract was treated with thiol-blocking reagents. This result was interpreted to indicate the presence of a binding protein. This study has demonstrated that inactive renin zymogen is different from so-called active big renin, which is a complex of active renin and the binding protein.

Animals↗
PubMed1981

A new protease in hog thyroid lysosomes. I. The presence of a leupeptin-sensitive protease in the soluble fraction of thyroid lysosomes.

The presence of protease activity at pH 7.5 and at acidic pH was demonstrated in the soluble fraction of lysosomes which were prepared from hog thyroid homogenates by subcellular fractionation. The ratios of specific activity measured at pH 7.5 to that at pH 3.5 were 0.07 to 0.08 for casein (at pH 7.5) or haemoglobin (at pH 3.5) as substrate and 0.13 for iodoamino acid-releasing activity from thyroglobulin as substrate. The protease activity measured at pH 7.5 was inhibited by inhibitors for neutral type protease, such as leupeptin, and by sulfhydryl inhibitors, such as iodoacetamide, indicating that the protease was a leupeptin-sensitive protease and contained a sulfhydryl group for its active site. Insensitiveness of the protease activity to di-isopropyl fluorophosphate excluded the involvement of a serine group at the active site. At pH 5.5 the proteolytic and iodoamino acid-releasing activities using casein and thyroglobulin, respectively, were also investigated. Several lines of evidence suggested that both activities measured at pH 5.5 were due to a mixture of acidic and leupeptin-sensitive protease activities.

Animals↗
PubMed1981

A new protease in hog thyroid lysosomes. II. A partial purification and characterization of a leupeptin-sensitive protease.

A leupeptin-sensitive new protease was partially purified from hog thyroid lysosomes. The purification procedure included solubilization by hypotonic treatment of lysosomes, and Sephacryl S-300 and Sephadex G-100 gel chromatography, and the purification ratio was 10-fold from lysosomes. The pH optimum of the protease activity was around 5.5 and its molecular weight was estimated to be 22 000 by gel filtration. 2-Mercaptoethanol activated the hydrolysis of protein substrates and its effect was most pronounced in the case of thyroglobulin as substrate. Among the inhibitors used, leupeptin, antipain, toluenesulfonyl-lysine chloromethyl ketone and, to a lesser degree, chymostatin and toluene-sulfonyl-phenylalanine chloromethyl ketone effectively inhibited the hydrolysis of casein by the enzyme at pH 5.5, whereas pepstatin did not inhibit the activity significantly. The enzyme activity was also inhibited by sulfhydryl inhibitors such as iodoacetamide, p-chloromercuribenzoate, and N-ethylmaleimide. The release of iodoamino acids from thyroglobulin by the enzyme was inhibited in the same manner by the inhibitors used in the hydrolysis of casein. The physiological role of the new protease is discussed in comparison with cathepsin B and L found in liver lysosomes.

Animals↗
PubMed1982

Release of prostaglandin I2 from hog kidney by propranolol.

Prostaglandin I2 (PGI2) decreases blood pressure. Perfusion of isolated hog kidney by propranolol in modified Krebs-Ringer solution resulted in a significant increase in 6-keto-prostaglandin F1 alpha, the major metabolite of PGI2. Prostaglandin E2 and renin activity remained unchanged. Because the concentration of PGI2-like substance in the renal vein has been shown to be greater than in the renal artery after bradykinin infusion, a contribution of PGI2 to the regulation of blood pressure was proposed. Isoproterenol has been shown to augment urinary kallikrein, but the effect of urinary kallikrein on propranolol is unclear. With a modified Krebs-Ringer solution free of plasma kininogen, a renin substrate, it was concluded that propranolol (1) induces PGI2 release from the kidney, which may contribute to a direct antihypertensive action of this beta-adrenergic blocking agent, and (2) decreases urinary kallikrein.

Animals↗
PubMed1982

One- and two-electron oxidations of tyrosine, monoiodotyrosine, and diiodotyrosine catalyzed by hog thyroid peroxidase.

Stopped flow experiments were carried out with purified hog thyroid peroxidase (A413 nm/A280 nm = 0.42). In the steady state of oxidations of L- and D-tyrosines, N-acetyltyrosinamide, and monoiodotyrosine, thyroid peroxidase existed in the form of Compound I, the primary catalytic intermediate of peroxidase in its reaction with H2O2. Kinetic results led us to conclude that thyroid peroxidase catalyzes two-electron oxidations of these molecules. In the steady state of oxidation of diiodotyrosine, on the other hand, the enzyme was found in the form of compound II at pH 7.4, but in the form of compound I at pH 5.5. The result implies that the mechanism of diiodotyrosine oxidation varied from a one-electron to a two-electron type as the pH decreased. The selection of mechanisms of oxidation appears to be peculiar to thyroid peroxidase; horseradish peroxidase and lactoperoxidase catalyzed only one-electron oxidations of these five donor molecules. Rate constants for rate-limiting steps in the reactions of these donor molecules with the three peroxidases were measured by overall kinetic and stopped flow kinetic methods.

Animals↗
PubMed1982

Structural homologies of cobalamin-binding proteins. Tryptic peptide mapping of intrinsic factor, transcobalamin and haptocorrin from man, hog and rabbit.

We have explored the structural features of cobalamin binding proteins by peptide mapping. The present report is a comparison of the radioiodinated tryptic peptides of intrinsic factor, transcobalamin and haptocorrin from man, hog and rabbit. The results show that the homology between analogous proteins from different species is close for intrinsic factor and transcobalamin and weaker for haptocorrin. The results also suggest the existence of one or more regions which, with minor changes, are conserved among all proteins investigated. This implies a common evolutionary origin for all the cobalamin binding proteins studied.

Animals↗
PubMed1981

Micro method for performing titration and neutralization test of hog cholera virus using established porcine kidney cell strain.

Hog cholera (HC) virus and antibody against it were estimated by the END method with microplates and CPK porcine kidney cell strain. To establish the technique of this method, studies were made on such basic conditions of the method as the type of strain of Newcastle disease virus (NDV), the time of challenge with this virus, and the concentration of serum in culture fluid. There was little difference in the infective titer of HC virus estimated between the END method performed by the established technique and the same method by the conventional technique with test tubes and swine testicle (ST) cells. Besides, there was a high correlation between the neutralizing antibody titer measured by the one technique and that measured by the other. The coefficient of correlation was r = +0.948 in this case. From the experimental results mentioned above it was concluded that the END method by the micro-technique with CPK cells was simpler than and as reliable as the same method conducted by any conventional technique, and that it was a practicable one capable of testing many samples.

Animals↗
PubMed1980

Atypical hog cholera infection: viral isolation and clinical study of in utero transmission.

Sows in different stages of pregnancy were inoculated with a low-virulence hog cholera strain. Clinical signs of disease were not observed in the sows during pregnancy, but most of their pigs were splaylegged and had nervous disorders; perinatal mortality was high. A few pigs from sows that were inoculated during the 1st trimester of pregnancy survived and remained inapparent carriers of virus, without developing antibodies. Seemingly, these pigs were immunotolerant. Virus was transmitted from immunotolerant pigs to susceptible pigs by contact 5 weeks after farrowing, but not 3 months after farrowing, despite the persistence of the virus at a high concentration in the blood and in the organs of the immunotolerant pigs.

Animals↗
PubMed1980

[Kinetics and thermodynamics of the hydrolysis-synthesis reaction of acetyl-L-methionine catalyzed by acylase I from hog kidney].

The kinetics and thermodynamics of the equilibrium reaction of hydrolysis--synthesis of acetyl-L-methionine catalyzed by acylase I from hog kidney were studied. At high concentrations of the products (acetate ion and L-methionine) the acetyl-L-methionine hydrolysis does not proceed to completion but to the equilibrium position. The equilibrium constant of hydrolysis determined at the attained equilibrium in both directions, i.e. hydrolysis and synthesis, is equal to 3.6 +/- 0.4. Based on the initial rates of hydrolysis and synthesis, a kinetic pattern for the dependence of the reaction rate on concentration of the components of the system is proposed. Evidence for this kinetic pattern is supported by the Holden ratio and the coincidence of the kinetic parameters calculated from the total kinetic curves and the initial rates of hydrolysis and synthesis of acetyl-L-methionine.

Amidohydrolases↗
PubMed1980

[Hog cholera diagnosis: an improved technique of seroneutralization based on use of a cytolytic virus strain in microplate (author's transl)].

An improved technique for the detection of hog cholera virus (HCV) neutralizing antibodies is described, in which running of the test is greatly facilitated by use of a cytolytic strain of HCV. This strain was isolated from persistently infected IB-RS 2, and was shown to induce a distinct cytopathic effect in several pig kidney cell lines (Laude, 1978). For the assay, serum samples at 1 : 10 are diluted serially twofold in disposable microplates, then 1 x 10(4) PFU of the virus-stock are added in each well. Trypsinized RP-TG cells are dispensed at 2 x 10(4)/well after 1 hour contact at 38 degrees C. After 4 days of incubation at 38 degrees C, plates are sequentially stained with neutral red and lugol, to make the undestroyed monolayers visualized. Neutralizing titre is expressed as the highest dilution of the serum affording a 75 percent protection of monolayer. This procedure has proved to be a labor saving technique yet being as reproducible and as sensitive as the immunofluorescence-tests. It combines the following advantages: 1) The immunofluorescence step is suppressed. 2) Results can be recorded without the aid of microscope. 3) The test is miniaturized. 4) Cultures of continuous cell lines are used. 5) The challenge virus is attenuated for the pig. Therefore this technique can be recommended for routine serological survey of the HCV-infection in pig-herds.

Animals↗
PubMed1981

Mucin degradation in human colon ecosystems. Degradation of hog gastric mucin by fecal extracts and fecal cultures.

The enteric flora of rats plays a major role in the degradation of their gut mucin glycoproteins, but the role of human enteric flora in degrading gut mucin glycoprotein has not been as well defined. We have studied the degradation of hog gastric mucin, which is structurally similar to human gastric mucin, in anaerobic human fecal cultures and by partially purified enzyme fractions from human fecal extracts and anaerobic culture supernates. Extensive degradation of the mucin carbohydrate moieties occurred in all systems, but the degradation of mucin protein was less. During a 48-h incubation, the average percent degradation of mucin carbohydrates and mucin protein were respectively 96% and 57% in eight fecal cultures, 66% and 15% by four fecal culture supernates, and 78% and 43% by three fecal extracts. Degradation of mucin protein was greater during bacterial growth in fecal cultures than during incubation with fecal culture supernates, suggesting that bacterial protease activity was predominantly cell bound. We conclude that, as in the rat, the human enteric microflora degrades mucin carbohydrate moieties extensively and the mucin protein to a lesser extent.

Adult↗