Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0847097 (acidity)
 15,165 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The influence of intramolecular catalysis and self-association on the kinetics of deamidation at the A-21 Asn residue of human insulin was explored at low pH and 35 degrees C. Observed rate constants of overall insulin degradation were determined as a function of pH over a pH range of 2.0-5.0 and as a function of total insulin concentration between pH 2.0-4.0. The pH-rate behavior of both monomeric and associated insulin degradation from pH 2.0 to 5.0 indicated intramolecular catalysis by the unionized carboxyl terminus of the A chain. Anhydride trapping with aniline at pH 3.0 provided evidence supporting the formation of a cyclic anhydride intermediate in the rate limiting step indicative of intramolecular nucleophilic catalysis. Insulin in the presence of aniline at low pH formed two anilide products, A-21 N delta 2-phenyl asparagine and N delta 2-phenyl aspartic acid human insulin, at the expense of desamido A-21 formation, consistent with the partitioning of a common intermediate. Self-associated insulin degraded at a rate approximately 2.5 times greater than that of the monomer at pH 2.0 and pH 3. However, self-association had a negligible or slight stabilizing effect on insulin decomposition at pH 4.0. An apparent downward shift in the pKa of the carboxyl terminus of approximately 0.75 units upon self-association and a catalytic rate constant which increases with -COOH acidity are proposed to account for these observations.
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PMID:The role of intramolecular nucleophilic catalysis and the effects of self-association on the deamidation of human insulin at low pH. 793 15

The objective of the present experiments was to study some properties of fowl spermatozoa which may play a role in the sperm storage and emptying mechanism of the uterovaginal sperm storage tubules (SST) of the hen. The effects exerted by different amino acids (aspartic acid, Asp; glutamic acid, Glu; gamma-aminobutyric acid, GABA; glycine, Gly) and by the pH of the environment at 24 and 39 degrees C on the motility and agglutination of cock spermatozoa were studied in vitro. The spermatozoa did not show agglutination in the presence of Asp and Glu, and became immobilised if the concentration of Glu or the acidity of the environment was increased. In neutral solutions of GABA and Gly or in a faintly alkaline solution characteristic plait-like conglomerations could be seen. The motility of spermatozoa immobilised by Glu could be restored in a varying degree by the addition of GABA or Gly. At a temperature of 24 degrees C, the spermatozoa became immobilised in a medium of pH 6.0 while showed maximum motility at pH 7.1. At 39 degrees C, the spermatozoa were immobilised at higher pH (6.2) and required a pH value as high as 7.4-7.5 to show the highest motility. Spermatozoa inactivated in an acidic solution could be immediately mobilised by alkalisation of the medium, irrespective of the Ca2+ content of the solution. Thus, Ca2+ was not found to play a role in the reactivation of spermatozoa. Nevertheless, marked differences were observed in the maintenance of sperm motility between solutions either containing or lacking Ca2+. As the concentration changes of the above-mentioned amino acids and the pH changes were found to affect the motility and agglutination of spermatozoa in vitro, they may influence also the regulatory mechanism of the uterovaginal SST during the egg-formation cycle in vivo.
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PMID:Motility and agglutination of fowl spermatozoa in media of different amino acid content and pH value in vitro. 890 46

Eight barrows (Yorkshire x [Finnish Landrace x Dutch Landrace]), initially 30 kg BW, were fitted with ileal cannulas to evaluate the effects of supplementing Ca benzoate (2.4%) and organic acids (OA) in the amount of 300 mEq acid/kg feed on dietary buffering capacity (BC), apparent digestibility and retention of nutrients, and manure characteristics. Swine were allotted in a 2 x 4 factorial arrangement of treatments according to a cyclic (8 x 5) changeover design. Two tapioca-corn-soybean meal-based diets were formulated without and with acidogenic Ca benzoate. Each diet was fed in combination with OA (none, formic, fumaric, or n-butyric acid). Daily rations were equal to 2.8 x maintenance requirement (418 kJ ME/BW(.75)) and were given in two portions. Chromic oxide (.25 g/kg) was used as a marker. On average, Ca benzoate lowered BC by 54 mEq/kg feed. This salt enhanced (P < .05) the ileal digestibility (ID) of DM, OM, arginine, isoleucine, leucine, phenylalanine, alanine, aspartic acid, and tyrosine (by up to 2.4 percentage units). Also, the total tract digestibility (TD) of DM, ash, Ca and GE, and Ca retention (percentage of intake) was greater (P < .05) in swine fed Ca benzoate, whereas N retention remained unaffected. Addition of all OA (formic and n-butyric acid, in particular) exerted a positive effect (P < .05) on the ID of amino acids (except for arginine, methionine, and cysteine). A similar effect (P < .05) was found for the TD of DM, OM, CP, Ca and total P and for the retention of N and Ca. In swine fed Ca benzoate, urinary pH decreased by 1.6 units (P < .001). In conclusion, dietary OA have a beneficial effect on the apparent ileal/total tract nutrient digestibilities, and Ca benzoate increased urine acidity, which could be effective against a rapid ammonia emission from manure of swine.
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PMID:The effects of calcium benzoate in diets with or without organic acids on dietary buffering capacity, apparent digestibility, retention of nutrients, and manure characteristics in swine. 1104 28

The effect of storage time on pH, titratable acidity, degrees Brix, organic acids, sugars, amino acids, and color of minimally processed cantaloupe melon (Cucumis melo L. var. reticulatus Naud. cv. Mission) was determined at 4 degrees C and 20 degrees C. Changes in most of the biochemical parameters with storage time were relatively slow at the lower temperature. At 20 degrees C, a 17% loss in soluble solids and a 2-fold increase in acidity occurred after 2 days. Organic acid content also increased considerably with time at this temperature as a result of the production of lactic acid. Oxalic, citric, malic, and succinic acids were the organic acids, and glucose, fructose, and sucrose were the sugars present in the freshly cut cantaloupe. Malic acid concentration decreased concurrently with lactic acid production indicating the possible involvement of anaerobic malo-lactic fermentation along with sugar utilization by lactic acid bacteria. The effect of storage on microbial growth was determined at 4, 10, and 20 degrees C. Gram-negative stained rods grew at a slower rate at 4 degrees C and 10 degrees C than the Gram-positive mesophilic bacteria that dominated microorganism growth at 20 degrees C. Eighteen amino acids were identified in fresh cantaloupe: aspartic acid, glutamic acid, asparagine, serine, glutamine, glycine, histidine, arginine, threonine, alanine, proline, tyrosine, valine, methionine, isoleucine, leucine, phenyl alanine, and lysine. The dominant amino acids were aspartic acid, glutamic acid, arginine, and alanine. Total amino acid content decreased rapidly at 20 degrees C, but only a slight decrease occurred at 4 degrees C after prolonged storage. Changes in lightness (L), chroma, and hue at both temperatures indicate the absence of browning reactions. The results indicate the potential use of lactic acid and lactic acid bacteria as quality control markers in minimally processed fruits.
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PMID:Biochemical and microbial changes during the storage of minimally processed cantaloupe. 1114 Dec 66

Different HLA class I alleles display a distinctive dependence on tapasin for surface expression and Ag presentation. In this study, we show that the tapasin dependence of HLA class I alleles correlates to the nature of the amino acid residues present at the naturally polymorphic position 114. The tapasin dependence of HLA class I alleles bearing different residues at position 114 decreases in the order of acidity, with high tapasin dependence for acidic amino acids (aspartic acid and glutamic acid), moderate dependence for neutral amino acids (asparagine and glutamine), and low dependence for basic amino acids (histidine and arginine). A glutamic acid to histidine substitution at position 114 allows the otherwise tapasin-dependent HLA-B4402 alleles to load high-affinity peptides independently of tapasin and to have surface expression levels comparable to the levels seen in the presence of tapasin. The opposite substitution, histidine to glutamic acid at position 114, is sufficient to change the HLA-B2705 allele from the tapasin-independent to the tapasin-dependent phenotype. Furthermore, analysis of point mutants at position 114 reveals that tapasin plays a principal role in transforming the peptide-binding groove into a high-affinity, peptide-receptive conformation. The natural polymorphisms in HLA class I H chains that selectively affect tapasin-dependent peptide loading provide insights into the functional interaction of tapasin with MHC class I molecules.
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PMID:A single polymorphic residue within the peptide-binding cleft of MHC class I molecules determines spectrum of tapasin dependence. 1281 74

Acid-neutralizing activity during amino acid fermentation by washed cells of Porphyromonas gingivalis, Prevotella intermedia and Fusobacterium nucleatum was studied. When the washed cells of these strains were anaerobically incubated in the presence of aspartylaspartic acid or glutamylglutamic acid for P. gingivalis, aspartic acid for P. intermedia and glutamic acid for F. nucleatum at an initial pH of 5.0 or 5.5, the pH of the incubation mixtures rose toward neutral. F. nucleatum had the highest acid-neutralizing activity, followed by P. intermedia and P. gingivalis. The P. intermedia and F. nucleatum cells were used to measure the amounts of base produced at a fixed pH of 5.0. These cells generated significant amounts of base at pH 5.0 along with the production of organic acids and ammonia from aspartic or glutamic acid. Acid-base balance theoretically calculated from the amounts of consumed substrate and end products implies that the acid-neutralizing activity was derived from the decrease in acidity during the fermentation of amino acid into organic acids and ammonia.
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PMID:Acid-neutralizing activity during amino acid fermentation by Porphyromonas gingivalis, Prevotella intermedia and Fusobacterium nucleatum. 1265 1

In this study we have sequenced peptides eluted from a truncated recombinant HLA-A*6602 molecule, and compared their features with data reported for peptides presented in the A*6601 molecule. A striking change in the amino-acid binding preferences was observed at peptide position P1, which interacts with pocket A of the HLA peptide-binding region. For A*6601, aspartic acid and glutamic acid, both of which possess polar acidic side-chains, have been described as auxiliary anchors. This is in marked contrast to A*6602, where we observed serine, which has a neutral polar side-chain, as auxiliary anchor at P1. Accordingly, this shift in the physico-chemical properties of the auxiliary anchor may be best explained by the HLA amino-acid polymorphism at position 163, where arginine (hydrophilic, alkaline) in A*6601 has been replaced by glutamic acid in A*6602. This amino-acid exchange results in a shift towards higher acidity in pocket A, apparently resulting in the loss of preference for acidic auxiliary anchors, and leading to the preference for the neutral amino acid serine. The change of the auxiliary anchor residue at P1 is likely to alter the spectrum of peptides presented by A*6602 compared with A*6601, which may result in allogenicity in the case of a mismatch in allogeneic stem cell transplantation.
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PMID:A single amino-acid polymorphism in pocket A of HLA-A*6602 alters the auxiliary anchors compared with HLA-A*6601 ligands. 1511 50

Changes in the taste of japonica, hybrid, and indica brown and milled rice, stored for 10 months at low (5 degrees C, 65-70% relative humidity) and room temperatures were observed by physicochemical analyses and a novel method using a taste sensing system. During storage, some properties increased or decreased while others were fairly constant. The main taste components of cooked rice such as sweetness (sucrose) and umami tastes (glutamic acid and aspartic acid) were reduced during storage, whereas glucose and fructose increased. The increase of fat acidity and consequent decrease of the pH value of the cooking solution may contribute to the off-taste of cooked stored rice. A taste sensing system with 10 lipid membrane sensors was also used to classify new and old rice samples using principal component analysis. Fresh and room temperature stored japonica and indica rice could be clearly distinguished; however, it was not possible to differentiate the samples stored at low temperature.
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PMID:Detection of changes in taste of japonica and indica brown and milled rice (Oryza sativa L.) during storage using physicochemical analyses and a taste sensing system. 1571 27

Using the in situ liver model system, we have recently shown that, after cholera toxin binding to hepatic cells, cholera toxin accumulates in a low-density endosomal compartment, and then undergoes endosomal proteolysis by the aspartic acid protease cathepsin-D [Merlen C, Fayol-Messaoudi D, Fabrega S, El Hage T, Servin A, Authier F (2005) FEBS J272, 4385-4397]. Here, we have used a subcellular fractionation approach to address the in vivo compartmentalization and cytotoxic action of cholera toxin in rat liver parenchyma. Following administration of a saturating dose of cholera toxin to rats, rapid endocytosis of both cholera toxin subunits was observed, coincident with massive internalization of both the 45 kDa and 47 kDa Gsalpha proteins. These events coincided with the endosomal recruitment of ADP-ribosylation factor proteins, especially ADP-ribosylation factor-6, with a time course identical to that of toxin and the A subunit of the stimulatory G protein (Gsalpha) translocation. After an initial lag phase of 30 min, these constituents were linked to NAD-dependent ADP-ribosylation of endogenous Gsalpha, with maximum accumulation observed at 30-60 min postinjection. Assessment of the subsequent postendosomal fate of internalized Gsalpha revealed sustained endolysosomal transfer of the two Gsalpha isoforms. Concomitantly, cholera toxin increased in vivo endosome acidification rates driven by the ATP-dependent H(+)-ATPase pump and in vitro vacuolar acidification in hepatoma HepG2 cells. The vacuolar H(+)-ATPase inhibitor bafilomycin and the cathepsin D inhibitor pepstatin A partially inhibited, both in vivo and in vitro, the cAMP response to cholera toxin. This cathepsin D-dependent action of cholera toxin under the control of endosomal acidity was confirmed using cellular systems in which modification of the expression levels of cathepsin D, either by transfection of the cathepsin D gene or small interfering RNA, was followed by parallel changes in the cytotoxic response to cholera toxin. Thus, in hepatic cells, a unique endocytic pathway was revealed following cholera toxin administration, with regulation specificity most probably occurring at the locus of the endosome and implicating endosomal proteases, such as cathepsin D, as well as organelle acidification.
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PMID:Role of receptor-mediated endocytosis, endosomal acidification and cathepsin D in cholera toxin cytotoxicity. 1745 37

The uptake of glyoxal by a variety of organic and inorganic aerosol types was examined in a Teflon chamber. Rapid glyoxal uptake was observed for all liquid-phase aerosols at all relative humidity levels tested (< 5 to 50% RH). Even for aerosol with known water content, Henry's Law cannot predict glyoxal uptake: H* > (3 +/- 1.5) x 10(8) mol kg(-1) atm(-1) for l-tartaric acid, H* > (1 +/- 0.5) x 10(8) for dl-malic acid and H* = (2 +/- 1) x 10(7) for malonic acid aerosol. Other liquid-phase aerosol particles containing amine functional groups (arginine, aspartic acid, and glutamic acid) took up even more glyoxal (H* > 3 x 10(8)). The trend of higher glyoxal uptake onto aerosol containing more nucleophilic organic compounds suggests that glyoxal is reacting with organic compounds in the aerosol phase. Solid-phase aerosol showed RH-dependent glyoxal uptake, likely due to the existence of surface water layers. However, particle growth rates were the highestfor sodium sulfate aerosol. For organic aerosol, growth rates correlated with the acidity of the carboxylic acid groups of the aerosol material, suggesting that glyoxal uptake is enhanced by mildly acidic conditions.
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PMID:Uptake of glyoxal by organic and Inorganic aerosol. 1860 66


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