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)

Glycoproteins were isolated in the contents of two sinus mucoceles by ionic exchange and gel filtration chromatography. These glycoproteins are of the mucin-type and characterized by their richness in carbohydrate, a low amino acid content with a strong proportion of hydroxy amino acids. However, they differ largely by their peptide axis, the length of the carbohydrate chain and their acidity, which is in relation with the presence of sialic acid residue and of sulfate groups. The least acidic mucins are the richest in sialic acid residue and in threonine but have the shortest carbohydrate chains while the most acidic are rich in sulfate, richer in serine and have longer carbohydrate chains. The wall of these two mucoceles has only one type of cell capable of synthetizing the glycoproteins: the epithelium goblet cells revealed by the PAS and the alcian blue at different pH. Glandular formations have never been found in the chorion.
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PMID:[Study of mucins of two sinus mucoceles (author's transl)]. 49 95

To evaluate the combined effects of threonine and glycine concentrations during growth on threonine aldolase activity (EC 2.1.2.1) of yogurt microorganisms, Streptococcus thermophilus and Lactobacillus bulgaricus, a modified milk growth medium was prepared using UF to deplete the free amino acid level. Threonine and glycine were added according to a 2x2x2 factorial design at 5 or 195 microg.ml(-1) along with a standard amino acid mixture. Acetaldehyde production and threonine aldolase activity were evaluated utilizing headspace gas chromatography. Results showed that threonine and glycine concentrations did not affect growth or titratable acidity. The high concentration of threonine in combination with low glycine in the growth medium resulted in increased acetaldehyde synthesis by both microorganisms. Conversely, high glycine with low threonine decreased acetaldehyde synthesis. High threonine and low glycine increased threonine aldolase activity of cell-free extracts from S. thermophilus and L. bulgaricus, whereas high glycine and low threonine reduced threonine aldolase activity of both microorganisms.
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PMID:Effect of threonine and glycine concentrations on threonine aldolase activity of yogurt microorganisms during growth in a modified milk prepared by ultrafiltration. 250 66

Factors affecting aspartimide formation, such as protecting groups, acidity, basicity, and temperature, were studied using the model tetrapeptide, Glu-Asp-Gly-Thr. The aspartyl carboxyl side chain in this tetrapeptide was either free or protected as a benzyl or cyclohexyl ester. Our results showed that the cyclohexyl ester led to far less aspartimide formation during acidic or tertiary amine treatment than the corresponding benzyl ester. The rate constants of aspartimide formation in HF-anisole (9:1, v/v) for the tetrapeptide protected as the benzyl ester were found to be 6.2 x 10(-6) and 73.6 x 10(-6) s-1 at -15 degrees and 0 degrees C respectively. These values were about three times faster than the corresponding free- or cyclohexyl ester-protected tetrapeptide. Little difference was seen when the studies were carried out at room temperature. The cyclohexyl protected tetrapeptide gave only 0.3% aspartimide in diisopropylethylamine treatment in 24 h, a 170-fold reduction of imide formation when compared with the benzyl protected tetrapeptide. Thus, using the cyclohexyl ester for aspartyl protection, our studies showed aspartimide formation could be significantly reduced to less than 2% under standard peptide synthesis conditions. Furthermore, with these model peptides, the mechanism of acid catalyzed aspartimide was studied in a range of HF concentrations. In dilute HF cleavage conditions (HF:dimethylsulfide 1:3, v/v), the mechanism was found to be of the AAC2 type, with the rate of aspartimide formation increasing very slowly with increasing acid concentration. In concentrated HF solutions (HF greater than 70% by volume), the rate of aspartimide formation increased rapidly with the increase in acid concentration. However, from model studies, the mechanism of aspartimide formation in concentrated HF was AAC2 rather than AAC1.
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PMID:Mechanisms of aspartimide formation: the effects of protecting groups, acid, base, temperature and time. 298 Jul 81

Snake insulin is isolated and crystallized from the pancreas of non-venomous snake (Zaocys dhumnades dhumnades, Cantor). The crystalline form is not rhombohedral but dodecahedral. The primary structure has been determined with the aid of an LKB solid-phase sequencer. In the primary structure of snake insulin, the presence of B5 Arg, B29 Arg, B16 Phe, B25 Tyr and B18 Ile is unusual in comparison with insulins from mammals, birds and fishes. However, the snake insulin we studied is very similar to rattle snake insulin, with the exception that A15 is glutamic acid instead of glutamine and B30 is threonine instead of serine. These differences are consistent with the higher acidity of the snake insulin we studied and with the threonine and serine content in amino acid analysis. The B10 residue of the snake insulin we studied is still histidine. The formation of dodecahedral crystals of the snake insulin has been discussed in connection with the presence of this histidine.
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PMID:The primary structure of snake (Zaocys dhumnades dhumnades, Cantor) insulin. 702 9

Leukocyte adhesion is a regulated process, which involves CD11/CD18 leukocyte integrins. CD11/CD18 acidity may be regulated intracellularly, and the CD18 polypeptide has previously been shown to become phosphorylated on serine and threonine after phorbol ester activation of T cells. Increased adhesiveness is believed to be mediated by regulating the overall avidity of cellular contact. CD11/CD18 integrins have earlier been reported to interact with several cytoskeletal proteins. We have now studied the involvement of the CD18 phosphorylation in cytoskeletal associations. We have investigated the distribution of phosphorylated CD18 between soluble, cytoskeletal and nuclear fractions of T cell detergent lysates. A significant amount of phosphorylated CD18 polypeptides was observed to fraction along with the cytoskeleton, while the majority of the cell surface CD18 molecules remained in the soluble fraction. Putative candidates for this altered cytoskeletal binding of CD11/CD18 were shown to be talin and filamin, which were observed to bind to CD18 cytoplasmic peptides and co-precipitate with CD18. The importance of the CD18 cytoplasmic domain in the regulation of the leukocyte adhesion was further strengthened by inhibition of phorbol ester-induced T cell adhesion with a phosphorylated lipopeptide corresponding to the cytoplasmic portion of the CD18. These results indicate that the induced CD18 phosphorylation and the altered cytoskeletal binding of the phosphorylated integrin complex may contribute to the increased avidity of CD11/CD18-mediated leukocyte adhesion.
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PMID:The cytoskeletal association of CD11/CD18 leukocyte integrins in phorbol ester-activated cells correlates with CD18 phosphorylation. 1042 73

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

Salmonella enterica serovar Typhimurium requires Mn(2+), but only a few Mn(2+)-dependent enzymes have been identified from bacteria. To characterize Mn(2+)-dependent enzymes from serovar Typhimurium, two putative PPP-family protein phosphatase genes were cloned from serovar Typhimurium and named prpA and prpB. Their DNA-derived amino acid sequences showed 61% identity to the corresponding Escherichia coli proteins and 41% identity to each other. Each phosphatase was expressed in E. coli and purified to near electrophoretic homogeneity. Both PrpA and PrpB absolutely required a divalent metal for activity. As with other phosphatases of this class, Mn(2+) had the highest affinity and stimulated the greatest activity. The apparent K(a) of PrpA for Mn(2+) of 65 microM was comparable to that for other bacterial phosphatases, but PrpB had a much higher affinity for Mn(2+) (1.3 microM). The pH optima were pH 6.5 for PrpA and pH 8 for PrpB, while the optimal temperatures were 45 to 55 degrees C for PrpA and 30 to 37 degrees C for PrpB. Each phosphatase could hydrolyze phosphorylated serine, threonine, or tyrosine residues, but their relative specific activities varied with the specific substrate tested. These differences suggest that each phosphatase is used by serovar Typhimurium under different growth or environmental conditions such as temperature or acidity.
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PMID:The PPP-family protein phosphatases PrpA and PrpB of Salmonella enterica serovar Typhimurium possess distinct biochemical properties. 1171 62

A series of Eu(III) metallopeptides, designed on the basis of the structural similarity of the helix-turn-helix and EF-hand motifs, have been studied by Eu(III) (7)F(0) --> (5)D(0) excitation spectroscopy. The impact of EF-hand ligand set differences on the hydration number and Eu(III) coordination environment are compared among the peptides. The conditional binding affinities were determined by Eu titration (P3, log K(a) = 6.0 +/- 0.4; P3W, log K(a) = 5.9 +/- 0.2; P5b, log K(a) = 5.3 +/- 0.1). Two similar coordination environments occur in each case, consistent with structural flexibility about the metal site. The coordination environments are consistent with 8- or 9-coordinate Eu(III), including six peptide-based ligands and two to three water molecules (P3, q = 1.9 +/- 0.2; P3W, q = 2.3 +/- 0.2; P4a, q = 1.9 +/- 0.3; P5b, q = 2.6 +/- 0.2). The Eu(III) (7)F(0) --> (5)D(0) excitation spectra are pH-dependent, as reported for several EF-hand proteins (oncomodulin, parvalbumin). A higher energy transition occurs at pH > 6, and has been assigned to deprotonation of coordinated water. The pK(a) leading to this new transition is dependent on Eu(III) Lewis acidity, which varies with the inner and outer sphere ligand set. The noncoordinating ninth position of the Eu-binding loop, which is poised to make second-sphere contacts to the coordinated water, stabilizes the deprotonated form of the coordinated solvent more effectively when it is Thr (P5b) than Asp (P3W). Upon DNA-binding by the metallopeptides, the pK(a) of the pH-dependent peak increases, but no new DNA-dependent transitions are observed. This indicates no DNA-based Eu(III) ligands are introduced, such as phosphate oxygen atoms of the DNA backbone. The hydration number decreases in the presence of DNA (P3W + DNA, q = 1.9 +/- 0.2; P5b + DNA, q = 1.7 +/- 0.2), indicating that DNA-binding by the metallopeptides organizes rather than compromises the Eu-binding site within the peptide.
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PMID:Europium luminescence of EF-hand helix-turn-helix chimeras: impact of pH and DNA-binding on europium coordination. 1463 31

A MUC1 type of glycopeptide was synthesized by the 9-fluorenylmethoxycarbonyl (Fmoc) solid-phase peptide synthesis (SPPS) protocol using benzyl and benzylidene-protected beta-D-Gal-(1-->3)-beta-D-GalNAc-Ser/Thr (TF-beta: a stereoisomer of the Thomsen-Friedenreich antigen). The synthetic glycopeptide was released from the resin with reagent K, and the resulting benzylated glycopeptide was deprotected under conditions of low-acidity trifluoromethanesulfonic acid (TfOH). The glycopeptide carrying duplicate non-natural O-glycans was dominant in the products, but was accompanied by a considerable amount of the glycopeptide missing one of the O-glycans. In contrast, the native alpha-glycoside was relatively stable under the acidic debenzylation conditions as shown by a parallel experiment with the glycopeptide involving alpha-D-GalNAc-Ser/Thr linkage. Enzymatic glycosylation with CMP-NeuAc was successful with both natural and non-natural O-glycans of the synthetic glycopeptide.
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PMID:Chemoenzymatic synthesis of a MUC1 glycopeptide carrying non-natural sialyl TF-beta O-glycan. 1703 Oct 43

The Rv3377c gene from the Mycobacterium tuberculosis H37 genome is specifically limited to those Mycobacterium species that cause tuberculosis. We have demonstrated that the gene product of Rv3377c is a diterpene cyclase that catalyzes the formation of tuberculosinol from geranylgeranyl diphosphate (GGPP). However, the characteristics of this enzyme had not previously been studied in detail with homogeneously purified enzyme. The purified enzyme catalyzed the synthesis of tuberculosinyl diphosphate from GGPP, but it did not bring about the synthesis of tuberculosinol. Optimal conditions for the highest activity were found to be as follows: pH 7.5, 30 degrees C, Mg(II) (0.1 mM), and Triton X-100 (0.1 %). Under these conditions, the kinetic values of K(M) and k(cat) were determined to be 11.7+/-1.9 microM for GGPP and 12.7+/-0.7 min(-1), respectively, whereas the specific activity was 186 nmol min(-1) mg(-1). The enzyme activity was inhibited at substrate concentrations higher than 50 microM. The catalytic activity was strongly inhibited by 15-aza-dihydrogeranylgeraniol and 5-isopropyl-N,N,N,2-tetramethyl-4-(piperidine-1-carbonyloxy)benzenaminium chloride (Amo-1618). The DXDTT(293-297) motif, corresponding to the DXDDTA motif conserved among terpene cyclases, was mutated in order to investigate its function. The middle D295 was found to be the most crucial entity for the catalysis. D293 and two threonine residues function synergistically to enhance the acidity of D295, possibly through hydrogen-bonding networks. The Rv3377c enzyme could also react with (14R/S)-14,15-oxidoGGPP to generate 3alpha- and 3beta-hydroxytuberculosinyl diphosphate. Conformational analyses were carried out with deuterium-labeled GGPP and oxidoGGPP. We found that GGPP and (14R)-oxidoGGPP adopted a chair/chair conformation, but (14S)-oxidoGGPP adopted a boat/chair conformation. Interestingly, the conformations of oxidoGGPP for the A-ring formation are the opposite of those of oxidosqualene when it is used as a substrate by squalene cyclases for the biosynthesis of hopene and tetrahymanol. (3R)-Oxidosqualene is folded in a boat conformation, whereas (3S)-2,3-oxidosqualene folds into a chair conformation, for the formation of the A-rings of the hopene and tetrahymanol skeletons, respectively.
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PMID:Characterization of the Rv3377c gene product, a type-B diterpene cyclase, from the Mycobacterium tuberculosis H37 genome. 1961 17


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