Search results for "Histidine"

showing 10 items of 152 documents

RP-HPLC Determination of Tiger Nut and Orgeat Amino Acid Contents

2005

The amino acid profile of 11 samples of tiger nuts ( Cyperus esculentusL.) grown in the area of “L'Horta Nord” in Valencia (Spain) and one sample of African origin were determined, along with the amino acid contents of 10 samples of natural orgeat from Valencia. Protein was hydrolysed by hydrochloric acid at 110 °C for 23 h, and amino acids were derivatised with AQC and determined by RP-HPLC with fluorescence detection. The chromatographic conditions were optimised. The analytical parameters (detection and quantification limits, precision and accuracy) showed the method to be sufficiently sensitive and reproducible for determining amino acids resistant to acid hydrolysis in tiger nuts and o…

chemistry.chemical_classificationChromatographyArginine010405 organic chemistryGeneral Chemical Engineeringdigestive oral and skin physiologyfungi010401 analytical chemistryfood and beveragesBiology01 natural sciencesHigh-performance liquid chromatographyIndustrial and Manufacturing Engineering0104 chemical sciencesAmino acidHydrolysischemistryAcid hydrolysisTyrosineEssential amino acidHistidineFood ScienceFood Science and Technology International
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Chiral recognition of protected amino acids by means of fluorescent binary complex pyrene/heptakis-(6-amino)-(6-deoxy)-β-cyclodextrin

2006

The ability of the binary complex pyrene (Py)/heptakis-(6-amino)-(6-deoxy)-β-cyclodextrin (am-β-CD) to act as a chiral selector was tested at two pH values (8.0 and 9.0). Phenylalanine (Phe), methionine (Met) and histidine (His) were used as chiral model molecules. The stability of ternary complexes Py/am-β-CD/amino acid was determined by means of spectrofluorimetric measurements. The data collected showed an increase in stability going from the binary to ternary complex and above all the possibility to use the binary complex as a chiral selector. Finally, data collected at two pH values showed that the binary complex is a better chiral selector when charged rather than in its neutral form.

chemistry.chemical_classificationCyclodextrinStereochemistryOrganic ChemistryPhenylalanineSettore CHIM/06 - Chimica OrganicaBiochemistryAmino acidchemistry.chemical_compoundchemistryDrug DiscoveryMoleculePyreneTernary operationTernary complexaminoacid chiral recognition cyclodextrinHistidineTetrahedron
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Staphylococcal NreB: an O2-sensing histidine protein kinase with an O2-labile iron-sulphur cluster of the FNR type

2004

Summary The nreABC ( n itrogen re gulation) operon encodes a new staphylococcal two-component regulatory sys- tem that controls dissimilatory nitrate/nitrite reduc- tion in response to oxygen. Unlike other two- component sensors NreB is a cytosolic protein with four N-terminal cysteine residues. It was shown that both the NreB-cysteine cluster and Fe ions are required for function. Isolated NreB was converted to the active form by incubation with cysteine desul- phurase, ferrous ions and cysteine. This activation is typical for FeS-containing proteins and was reversed by oxygen. During reconstitution an absorption band at 420 nm and a yellow-brownish colour (typical for an FNR-type iron-sul…

chemistry.chemical_classificationOperonBiologyMicrobiologyFerrousEnzymeBiochemistrychemistryThiolKinase activityProtein kinase AMolecular BiologyHistidineCysteineMolecular Microbiology
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Citrate Sensing by the C 4 -Dicarboxylate/Citrate Sensor Kinase DcuS of Escherichia coli : Binding Site and Conversion of DcuS to a C 4 -Dicarboxylat…

2007

ABSTRACT The histidine protein kinase DcuS of Escherichia coli senses C 4 -dicarboxylates and citrate by a periplasmic domain. The closely related sensor kinase CitA binds citrate, but no C 4 -dicarboxylates, by a homologous periplasmic domain. CitA is known to bind the three carboxylate and the hydroxyl groups of citrate by sites C1, C2, C3, and H. DcuS requires the same sites for C 4 -dicarboxylate sensing, but only C2 and C3 are highly conserved. It is shown here that sensing of citrate by DcuS required the same sites. Binding of citrate to DcuS, therefore, was similar to binding of C 4 -dicarboxylates but different from that of citrate binding in CitA. DcuS could be converted to a C 4 -…

chemistry.chemical_classificationPeriplasmic spacePlasma protein bindingBiologymedicine.disease_causeMicrobiologychemistry.chemical_compoundEnzymechemistryBiochemistrymedicineBinding siteCitric acidMolecular BiologyEscherichia coliPeptide sequenceHistidineJournal of Bacteriology
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Multiscale Simulations of SARS-CoV-2 3CL Protease Inhibition with Aldehyde Derivatives. Role of Protein and Inhibitor Conformational Dynamics in the …

2020

<p>We here investigate the mechanism of SARS-CoV-2 3CL protease inhibition by one of the most promising families of inhibitors, those containing an aldehyde group as warhead. These compounds are covalent inhibitors that inactivate the protease forming a stable hemithioacetal complex. Inhibitor 11a is a potent inhibitor that has been already tested in vitro and in animals. Using a combination of classical and QM/MM simulations we determined the binding mode of the inhibitor into the active site and the preferred rotameric state of the catalytic histidine. In the noncovalent complex the aldehyde group is accommodated into the oxyanion hole formed by the NH main chain groups of residues …

chemistry.chemical_classificationProteasebiologyStereochemistrymedicine.medical_treatmentActive siteHemithioacetalAldehydechemistry.chemical_compoundchemistryNucleophileCovalent bondmedicinebiology.proteinOxyanion holeHistidine
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Salt effects on the protonation of l-histidine and l-aspartic acid: a complex formation model

1991

Abstract Protonation constants of l -histidine (histidinate: his − ) and l -aspartic acid (aspartate: asp 2− ) were determined potentiometrically, using the (H + ) glass electrode, in aqueous tetraethylammonium iodide (Et 4 NI), calcium chloride and sodium chloride solutions, at 0 −3 and 10 ⩽, T ⩽, 45 ° C. Differences in protonation constants determined in different salt media were explained by a complex formation model and, according to this model, the presence of the following species was hypothesized: Ca(his) + , CaH(his) 2+ , CaH 2 (his) 3+ Na(his) 0 , H 3 (his)X + , H 2 (his)X 0 , Et 4 N(his) 0 , Et 4 NH(his) + , Ca(asp) 0 , CaH(asp) + , CaH 2 (asp) 2+ , Na(asp) − , NaH(asp) 0 , H 3 (a…

chemistry.chemical_classificationTetraethylammonium iodideAqueous solutionendocrine system diseasesSodiumInorganic chemistrychemistry.chemical_elementProtonationCondensed Matter PhysicsMedicinal chemistrychemistry.chemical_compoundDicarboxylic acidchemistryIonic strengthAspartic acidPhysical and Theoretical ChemistryInstrumentationHistidineThermochimica Acta
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Interaction of Dimethyltin(IV)2+ Cation with Gly-Gly, Gly-His, and Some Related Ligands. A New Case of a Metal Ion Able To Promote Peptide Nitrogen D…

1999

Equilibrium (pH-metric) and spectroscopic (1H,13C, and 119Sn NMR and 119Sn Mossbauer) studies were performed to characterize the interaction of the dimethyltin(IV) cation with glycine, glycyl-glycine (Gly-Gly), imidazole-4-acetic acid, histamine, histidine, glycyl-histamine, glycyl-histidine (Gly-His), and β-alanyl-histidine (carnosine). For histamine and glycyl-histamine (having only nitrogen donor atoms) no complex formation was detected. The hydrolyzed species of the dimethyltin(IV) cation are always dominant over the complexes formed with the other ligands, except with Gly-Gly and Gly-His. For these two ligands, {COO-,N-,NH2} coordinated complexes are dominant in the neutral pH range wi…

chemistry.chemical_classificationanimal structuresAqueous solutionintegumentary systemInorganic chemistryPeptideMedicinal chemistryInorganic ChemistryMetalchemistry.chemical_compoundTrigonal bipyramidal molecular geometryDeprotonationchemistryvisual_artembryonic structuresvisual_art.visual_art_mediumChelationCarboxylatePhysical and Theoretical ChemistryHistidineInorganic Chemistry
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Mechanisms of photosensitization by drugs: Involvement of tyrosines in the photomodification of proteins mediated by tiaprofenic acid in vitro

1997

The photosensitizing potential of drugs must be related to their photoreactivity towards the target biomolecules. In this context, a representative photosensitizing drug (tiaprofenic acid) was co-irradiated with a model protein, bovine serum albumin (BSA). This led to a significant degree of protein crosslinking and to the formation of trace amounts of drug-BSA photoadducts. Amino acid analysis of the hydrolysed (HC1) protein showed that His and Tyr undergo a dramatic decrease (approx. 90%) as a consequence of drug-mediated photodynamic processes. When the drug was irradiated in the presence of the pure amino acids, extensive phototransformation of the latter was observed. Other photosensit…

chemistry.chemical_classificationbiologyChemistrySerum albuminContext (language use)General MedicineToxicologyAmino acidMechanism of actionBiochemistrymedicinebiology.proteinmedicine.symptomTyrosineBovine serum albuminTiaprofenic acidHistidinemedicine.drugToxicology in Vitro
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DRUG-DRUG INTERACTIONS VIA INHIBITION OF MICROSOMAL ENZYMES INVOLVED IN METABOLISM OF EPOXIDES PRODUCED BY MICROSOMAL MONOOXYGENASE

1977

SUMMARY Benzo(a)pyrene was activated by liver microsomes to mutagens detected by the reversion of histidine dependent Salmonella typhimurium TA 1537. Using pure epoxide hydratase or epoxide hydratase inhibitors, comparing animal species with high and low epoxide hydratase activity, or inducing monooxygenase activity, it was shown that epoxide hydratase was a critical enzyme for the inactivation of these mutagens. Many clinically used drugs are metabolized to epoxides. Epoxides are not necessarily mutagenic, but since epoxide hydratase has a very low substrate specificity, such epoxides may competitively inhibit the hydration of mutagenic epoxides, as demonstrated in the present study for th…

chemistry.chemical_classificationchemistry.chemical_compoundEnzymeNon-competitive inhibitionchemistryBiochemistryStereochemistryReversionEpoxidePyreneMetabolismEpoxide hydrolaseHistidine
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ARGININE, HISTIDINE AND TRYPTOPHAN IN PEPTIDE SYNTHESIS. THE IMIDAZOLE FUNCTION OF HISTIDINE

1989

chemistry.chemical_compoundArginineChemistryStereochemistryOrganic ChemistryTryptophanPeptide synthesisImidazoleHistidine decarboxylaseHistidineFunction (biology)Organic Preparations and Procedures International
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