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At least 253 records · Page 14Linked to original sources
PubMed1977

Branched blood group A-active fucolipids of hog gastric mucosa.

New complex glycolipids have been extracted from hog gastric mucosa with the mixture of 0.4 M sodium acetate in methanol/chloroform/water. Three A-active fucolipids having branched carbohydrate chains have been purified from this extract. The postulated structures of these glycolipids are based on the results of partial acid hydrolysis, oxidation with periodate and chromium trioxide, and permethylation studies.

ABO Blood-Group System↗
PubMed1988

Aminoacylase I from hog kidney: anion effects and the pH dependence of kinetic parameters.

The hydrolysis of acetylamino acids by highly purified hog kidney aminoacylase I (N-acylamino acid amidohydrolase, EC 3.5.1.14) was investigated using flow injection analysis to determine reaction rates. We show that the distinctly bell-shaped pH versus activity profiles observed in previous studies do not reflect protonic equilibria in the enzyme, but were created by buffer effects. At low pH, anions such as phosphate, nitrate or chloride markedly increase Km. These effects are reversed at higher pH. In zwitterionic 'Good' buffers (Mes, Mops, and Bicine), maximal velocities are almost independent of pH between 6.5 and 9 for all substrates studied (Ac-LAla, Ac-LGlu, Ac-LMet, Ac-LPhe). Below pH 6.5, the catalytic constants decrease with pH, apparently due to the protonation of a carboxylate with a pKa of 5.5-6. The pH dependence of Km markedly varies among different substates. We conclude that the observed profiles all result from the dissociation of an active-site residue with a pKa of 8-8.5, which we tentatively identify as an active-site cysteine residue. A working model of aminoacylase catalysis is presented that accounts for most of the known facts.

Amidohydrolases↗
PubMed1971

Number and types of peptide chains in thyroglobulin: tryptic peptides of noniodinated hog thyroglobulin.

In order to identify the number and types of peptide chains in thyroglobulin, noniodinated 19-S thyroglobulin obtained from goitrogen-treated hogs was exhaustively digested with trypsin (EC 3.4.4.4) after reduction and S-carboxymethylation. The digestion mixture was preliminarily separated into 30 fractions on Sephadex G-100 or G-15 and SE-Sephadex columns. The number of various tryptic peptides contained in each fraction was determined on peptide maps, where spots were detected with ninhydrin for total peptides and with each specific reagent for arginine, histidine or tyrosine-containing peptides. The number of total peptides observed in most of the fractions was estimated to be half the number of lysine plus arginine residues found in each fraction per mole of thyroglobulin, and the number of specific peptides was also close to half the number of each specific amino acid. These findings imply that thyroglobulin has 2-fold symmetry in the structure at the level of tryptic fragments and thus probably at the level of intact peptide chains.

Amino Acids↗
PubMed1975

Purification of hog renin by affinity chromatography using the synthetic competitive inhibitor (D-Leu6)octapeptide.

The renin substrate analog His-Pro-Phe-His-Leu-D-Leu-Val-Tyr ([D-Leu6]-octapeptide) acts as a potent inhibitor of renin because of the D-amino acid substitution at the cleavage site. This inhibitor was coupled to CNBr-activated Sepharose 4B to yield a support for affinity chromatography. Hog renin with a specific activity of 1.2 Goldblatt units/mg was in one step purified 195-fold to a final specific activity of 234 Goldblatt units/mg. Application of a pH gradient from 5.0 to 7.5 to the support was found to be the most successful elution program, probably because the [D-Leu6]-octapeptide is not an inhibitor for renin at neutral pH.

Animals↗
PubMed1976

The presence of N-terminal pyroglutamyl residues in hog thyroglobulin.

A method was devised to isolate N-terminal peptide fragments from the polypeptide chains constituting thyroglobulin even in the case when the terminal amino groups are naturally blocked, for instance, acylated. Reduced and carboxymethylated hog thyroglobulin was first acetylated and digested with thermolysin. The blocked N-terminal peptide fragments were separated from the unblocked N-terminal fragments by column chromatography on Dowex 50, then on Dowex 1 after dinitrophenylation, and finally fractionated into ten fractions by paper chromatography after gel filtration on Sephadex G-10. Structural analyses by enzymic or partial acid hydrolysis of these peptide fractions failed to detect N-terminal acetyl amino acid. Instead, pyroglutamyl peptides including pyroglutamylleucine were found. By the same method, acetylated lysine and glycine were identified for chicken lysozyme and horse myoglobin, respectively. The use of thermolysin because of its unique specificity, and the possible relevance of the present result to the previous data on the N-terminal analysis of thyroglobulin are discussed.

Amino Acid Sequence↗
PubMed1984

Insulin modulates thyrotropin-induced follicle reconstruction and iodine metabolism in hog thyroid cells cultured in a chemically defined medium.

Effects of insulin on cultured hog thyroid cells were examined in a chemically defined medium supplemented with thyrotropin. Thyrotropin-induced follicle reconstruction and recovery of functional activities were stimulated by the addition of insulin to the culture medium. The iodide uptake and organification at the maximum stimulation exceeded 3 times those of the control values. The minimum effective dose of insulin was 60 microU/ml. The insulin stimulation occurred after a latency period of 24 h. Since no growth promoting effect of insulin was observed during the cultivation period in the present study, insulin appears to act in concert with thyrotropin in regenerating the characteristic properties of the differentiated cells during cultivation.

Animals↗
PubMed1990

N-terminus determination: FAD and NADP binding domain mapping of hog liver flavin-containing monooxygenase by tandem mass spectrometry.

Highly purified hog liver flavin-containing monooxygenase was sequentially denatured, reduced, carboxymethylated, and digested with endoproteinase Glu-C. The purified peptides were subjected to mass spectrometric analysis and the amino acid sequence of selected fragments was determined by tandem mass spectrometry. The amino acid sequence of the first 12 residues of the N-terminus was: Ac-Ala-Lys-Arg-Val-Ala-Ile-Val-Gly-Ala-Gly-Val-Ser-Gly. The amino acid sequence determined for another peptide was: Lys-Ser-Val-Leu-Val-Val-Gly-Met-Gly-Asn-Ser-Gly-Thr-Asp-Ile-Ala-Val-Glu. The results provide direct evidence for the structure of the N-terminal modification of the protein and for the existence of the FAD and NADP binding domains of Gly-X-Gly-X-X-Gly.

Acetylation↗
PubMed1982

Relationship between cyclic AMP-dependent protein kinase activation and Ca uptake increase of sarcoplasmic reticulum fraction of hog biliary muscles relaxed by cholecystokinin-C-terminal peptides.

In hog terminal bile duct cholecystokinin peptides caused an activation of cyclic AMP-dependent protein kinase (A-PK) with cyclic AMP, followed by increase in Ca uptake of sarcoplasmic reticulum fraction (SR-F). By contrast, papaverine showed no activation of A-PK-induced Ca uptake by SR-F with cyclic AMP. The Ca uptake by SR-F was dependent on ATP and Mg2+, but the component phosphorylated was not the phosphoenzyme intermediate in Ca2+-ATPase. The effect of Ca uptake was blocked by the inclusion of a protein inhibitor of A-PK. The correlation coefficient between cyclic AMP-dependent SR-F phosphorylation and stimulated Ca uptake by the phosphorylated SR-F was 0.731 (P less than 0.01). These results suggest that one of the mechanisms by which CCK-4, CCK-8, and CCK-33 peptides relax isolated Oddi's sphincters of terminal bile ducts is activation of A-PK-induced Ca uptake by sarcoplasmic reticulum fraction and possibly also by plasma membrane.

Animals↗
PubMed1983

Evidence that relaxation of hog biliary muscle is mediated by the interaction between the protein inhibitor of cyclic AMP dependent protein kinase and cholecystokinin C-terminal peptides.

The interaction of various cholecystokinin (CCK) peptides with the protein inhibitor (PK-I) of cyclic AMP dependent protein kinase (A-PK) has been studied. The order of the affinities (ED50) for relaxation of hog biliary muscle by a series of C-terminal peptides of CCK correlated with the order of the potencies for A-PK-catalyzed phosphorylation of the sarcoplasmic reticulum enriched fraction (SR-F) in the muscle. CCK-4 peptide inhibited the PK-I of A-PK. The apparent Km value of the peptide was 11.5 microM. Scatchard plot analysis for the binding of [14C]CCK-6 peptide to the PK-I showed a dissociation constant (Kd) of 11.2 microM. These results indicated that the Kd value agreed with the ED50 value of CCK-6 and the Km value of CCK-4. It is proposed that a receptor for CCK C-terminal peptides is probably a component in the PK-I; binding of the peptides to this site usually results in the relaxation by these allosteric inhibitors of the PK-I.

Animals↗
PubMed1987

Actions of antisecretory agents on proton transport in hog gastric microsomes.

The properties of K+-stimulated ATP hydrolysis (K+-ATPase) and vesicular accumulation of H+ (H+ accumulation) in hog gastric microsomes were investigated. The microsomes consisted of smooth surfaced vesicular particles, 70-300 nm in diameter. Both the activities of ATPase and the vesicular accumulation of H+ were stimulated by K+ in the presence of Mg2+, and enhanced by the K+-ionophore, valinomycin. However, there were differences in regulation of K+-ATPase and H+ accumulation by K+ ions, i.e. K+ at concentrations higher than 10 mM decreased K+-ATPase activity but further enhanced H+ transport. This observation suggests that the two reactions are partly independent. The H+ accumulation was inhibited by omeprazole, fenoctimine, spermine, and NaSCN, but not by cimetidine, prostaglandin E2, and atropine. The inhibitory effect of omeprazole on H+ accumulation paralleled the inhibition of K+-ATPase, while fenoctimine, spermine, and NaSCN suppressed H+ accumulation, without inhibiting K+-ATPase, under appropriate concentrations. In addition, the spontaneous diffusion of H+ across the microsomal membrane was markedly enhanced by fenoctimine, but not by the other agents used. These results indicate that omeprazole inhibits H+ accumulation by inhibiting K+-ATPase, fenoctimine suppresses H+ accumulation mainly by increasing the loss of accumulated H+ from the microsomal vesicles, spermine and NaSCN reduce H+ accumulation by inhibiting the transport of H+ into microsomal vesicles.

Adenosine Triphosphatases↗
PubMed1987

Studies on substrate specificity of the hog liver flavin-containing monooxygenase. Anionic organic sulfur compounds.

The influence of anionic groups on interaction of nucleophilic sulfur compounds with the purified hog liver flavin-containing monooxygenase was evaluated from kinetic constants obtained with various dithiobenzoates, thiolbenzoates, and thiolalkylcarboxylic acids. All compounds tested bearing a single negative charge localized on sulfur were excellent substrates but derivatives with a carboxylic acid group one or two carbons removed from the heteroatom exhibited low or no substrate activity. The effect of a carboxylic acid group more distal from sulfur appeared to depend on steric factors that are not well defined. For instance, none of the carboxylic acids (C2-C8) bearing a single thiol on the terminal carbon were oxygenated at detectable rates, whereas dihydrolipoic acid appeared to be a substrate although the concentration required for half-maximal activity was quite high (approximately 2 mM). Lipoic acid was a much better substrate (Km = 0.12 mM), and kinetic constants obtained with lipoic acid analogues suggest that position of the negative charge relative to the dithiolane ring is critical, since increasing the length of the side chain increased the Km. None of the alicyclic disulfides or sulfides containing one or more carboxylic acid groups showed detectable substrate activity. However, the more lipophilic sulfur-containing fatty acids inhibited the enzyme which may mask their potential substrate activity.

Animals↗
PubMed1980

Renin and prorenin in hog brain: ubiquitous distribution and high concentration in the pituitary and pineal.

With the objective of clarifying the nature of renin-like activity in the brain, we have devised methods to distinguish true renin from acid protease. These methods were used to determine the regional distribution of true renin in hog brain. The pineal was found to be the richest source of renin followed by the adenohypophysis and choroid plexus. The hypothalamus, cerebellum and amygdala contained moderately high concentrations of renin. Renin concentration in the neurohypophysis was negligible. Many regions contained activatable prorenin. The molecular weight and the pH-dependence of the brain renin were identical to these same properties of renal and plasma renins. Based upon its specific affinity to concanavalin A, brain renin was judged to be a glycoprotein. The electrofocusing pattern of renin from different regions of the brain differed from that of plasma and kidney renins, a discrepancy which could be interpreted as evidence for the endogenous synthesis of renin in the brain.

Angiotensin I↗
PubMed1977

Structural studies on branched fucosphingolipids of hog gastric mucosa.

A structural studies have been performed on new complex glycolipids extracted from hog gastric mucosa by 0.4 M sodium acetate in methanol-chloroform-water, and which were purified to homogeneity by DEAE-Sephadex and Florisil column chromatography and by preparative thin-layer chromatography in three solvent systems. Five branched fucolipids have been purified from this extract, three of which have been characterized previously [1] and remaining two were subject of this investigations. Based on the results of partial acid hydrolyses, oxidation with periodate and chromium trioxide, permethylation and serological activities following structures were proposed.

Animals↗
PubMed1987

Proglumide peptides and CCK antagonistic action in hog duodenal circular muscle.

New proglumide peptides were synthesized and their inhibitory activity against the cholecystokinin (CCK)-induced relaxation was tested in duodenal circular muscles of hogs in order to locate the active moiety. Isotonic tension is reported as a percentage of the relaxation induced by CCK-4 (4.23 microM) or by Ca-free EGTA (2 mM). In R1-CONHCH(CH2CH2CO-R2)CON(CH2CH2CH3)2, P2-II(R1 = PhCH2O, R2 = Phe33-NH2), its D isomer and P3-I (R1 = Ph, R2 = Asp32-Phe33-NH2) had potent antagonistic activity (IC50 = 47.9 (32.4-72.4) microM, 25.1 (10.0-61.7) microM and 186 (141-240) microM, respectively). Benzotript, from another group of CCK antagonists had an IC50 of 52.5 (40.7-67.6) microM. P2-II (49 microM) or its D isomer (19.6 microM) antagonized non-competitively, and P3-I (168 microM) and benzotript (58.4 microM) antagonized competitively the CCK-4-induced relaxation. P3-I (84 or 168 microM) also antagonized competitively the CCK-8-induced relaxation. The amino acids of Tyr27, Trp30 and Phe33, separately, play important roles for agonist activity for relaxation. Tyr27 is the main relaxing group, Trp30 an antagonistic one and Phe33 is another relaxing one. In the proglumide skeleton, N,N-dipropylglutaramic acid acts like Trp30. Agonist, partial agonist and antagonist activities are exerted by these three groups and bulky substituents.

Animals↗
PubMed1989

Resonance Raman characterization of hog thyroid peroxidase. An SERRS study.

Resonance Raman (RR) spectra of hog thyroid peroxidase (TPO) were observed for the first time and compared with those of lactoperoxidase (LPO) and horseradish peroxidase (HRP). Since TPO purified by monoclonal antibody-assisted immunoaffinity chromatography was strongly fluorescent, the surface enhancement technique using Ag colloid adsorption was used for the oxidized form, but ordinary RR spectra could be obtained for the reduced form. The RR spectra of TPO were distinct from those of HRP in both the oxidized and reduced states and indicated the presence of six-coordinated iron-protoporphyrin.

Animals↗
PubMed1970

Effect of sialidase on blood group specificity of hog submaxillary glycoproteins.

Hogs can be divided into three phenotypes A, H and In, depending on the ability of extracts of their submaxillary glands to inhibit the agglutination of human A cells with human anti-A, and human O cells with eel-anti-H serum. Evidence is here provided that the inactive glycoprotein, In, represents H active glycoprotein containing additional N-glycolyl neuraminic acid, which stereospecifically masks the H determinant, alpha (1 --> 2)-L-fucosyl residue.

Journal Article↗
PubMed1993

A novel beta-N-acetylglucosaminidase activity in hog gastric mucosal microsomes: preferential hydrolysis of terminal GlcNAc beta 1-3 linkages in GlcNAc beta 1-3(GlcNAc beta 1-6)Gal beta 1-4GlcNAc, but GlcNAc beta 1-6 linkages in GlcNAc beta 1-3(GlcNAc beta 1-6)Gal.

Hog gastric mucosal microsomes contain beta-N-acetylglucosaminidase activity which cleaves GlcNAc beta 1-3(GlcNAc beta 1-6)Gal beta 1-4GlcNAc at the terminal GlcNAc beta 1-3Gal linkage faster than at the GlcNAc beta 1-6Gal bond, producing mainly GlcNAc beta 1-6Gal beta 1-4GlcNAc. In a marked contrast, GlcNAc beta 1-3(GlcNAc beta 1-6)Gal is cleaved primarily at the GlcNAc beta 1-6Gal bond, while partial hydrolysis of GlcNAc beta 1-3(GlcNAc beta 1-6)Gal beta 1-4Glc reveals similar rates of cleavage for the (1-3) and (1-6) linkages. Our data support the notion that the terminal beta 1,6-linked GlcNAc unit of GlcNAc beta 1-3(GlcNAc beta 1-6)Gal beta 1-4GlcNAc may interact with the reducing end GlcNAc unit intramolecularly in water solution.

Acetylglucosaminidase↗
PubMed1984

Synergic effects of kallikrein-kinin and prostaglandins on renin release on infusion of isolated hog kidney with aldosterone.

The effects of infusion of a large amount of aldosterone into the renal artery of isolated perfused hog kidney on the release of renin, prostaglandins (PG) and kinin and the excretion of urinary kallikrein were investigated. Infusion of aldosterone at a rate of 100 ng/min (100 to 800 ng/ml of perfusate) resulted in significant releases of renin, PG (PGE2 , 6-0-PGF1 alpha), and kinin and increase in urinary kallikrein. Infusion of aldosterone and an inhibitor of kallikrein, aprotinin, decreased the releases of renin, PG and kinin and infusion of aldosterone with indomethacin decreased the release of PG but increased that of kinin and urinary kallikrein without significant change in renin releases. These findings suggest that the release of renin by aldosterone may result from synergic effects of renal PG and the kallikrein -kinin system.

Aldosterone↗