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TNP-ATP (2'-(or-3')-O-(Trinitrophenyl) Adenosine 5'-Triphosphate, Trisodium Salt)
El análogo nucleótido TNP-ATP está modificado en la fracción de ribosa y es esencialmente no fluorescente en el agua. LosMás información
| Número de catálogo | Cantidad |
|---|---|
| T7602 | 2 mL |
Número de catálogo T7602
Precio (MXN)
-
Cantidad:
2 mL
El análogo nucleótido TNP-ATP está modificado en la fracción de ribosa y es esencialmente no fluorescente en el agua. Los nucleótidos de la TNP experimentan una transición de equilibrio a una estructura semiquinoide que tiene propiedades espectrales de longitud de onda relativamente larga; esta forma solo es fluorescente cuando se une al sitio de unión de nucleótidos de algunas proteínas.
Para uso exclusivo en investigación. No apto para uso en procedimientos diagnósticos.
Especificaciones
Etiqueta o tinteTNP
Tipo de productoTNP-ATP
Cantidad2 mL
Condiciones de envíoHielo húmedo
Unit Size2 mL
Contenido y almacenamiento
Almacenar en el congelador de -5 °C a -30 °C y proteger de la luz.
Preguntas frecuentes
What is the concentration of TNP-ATP (2'-(or-3')-O-(Trinitrophenyl) Adenosine 5'-Triphosphate, Trisodium Salt) (Cat. No. T7602)?
Citations & References (250)
Citations & References
Abstract
Fluorescence resonance energy transfer mapping of the fourth of six nucleotide-binding sites of chloroplast coupling factor 1.
Journal:J Biol Chem
PubMed ID:1832671
Equilibrium dialysis measurements of adenine nucleotide binding to chloroplast coupling factor 1 suggest that the enzyme has six binding sites for ADP, adenylyl-beta,gamma-imidodiphosphate (AMP-PNP), and 2'(3')-O-2,4,6-trinitrophenyl-ATP (TNP-ATP). High affinity binding at all six sites requires the divalent cation, Mg2+. Three of the nucleotide-binding sites, sites 1, 2, and 3, have
Site-site interaction on mitochondrial F1-ATPase. Functional symmetry of the high-affinity nucleotide binding sites.
Journal:Biol Chem Hoppe Seyler
PubMed ID:2876715
Interactions between the high affinity binding sites on mitochondrial F1 were analysed by combined use of the nucleotide analogues 3'-O-(1-naphthoyl)-ADP (N-ADP) and 2'-3'-O-(2,4,6-trinitrophenyl)-ADP (TNP-ADP). The binding behaviour of F1 with respect to these ligands was studied by measuring the fluorescence of F1 and of TNP-ADP and the fluorescence anisotropy of
Mitochondrial ATP synthase. cDNA cloning, amino acid sequence, overexpression, and properties of the rat liver alpha subunit.
Journal:J Biol Chem
PubMed ID:2137825
'The predicted amino acid sequence of the alpha subunit of the rat liver mitochondrial ATP synthase has been obtained by sequencing a cDNA for the alpha subunit. Analysis of the sequence shows that it contains the A and B consensus sequences found in many nucleotide-binding proteins. Twelve amino acids of
Elimination of the hydroxyl groups in the ribose ring of ATP reduces its ability to phosphorylate the sarcoplasmic reticulum Ca(2+)-ATPase.
Journal:J Biol Chem
PubMed ID:8463222
'2''-Deoxyadenosine 5''-triphosphate, 3''-deoxyadenosine 5''-triphosphate, and 3''-amino-3''-deoxyadenosine 5''-triphosphate were substituted for ATP in the Ca2+ pumping cycle of the sarcoplasmic reticulum Ca(2+)-ATPase. The rate of phosphorylation of the enzyme decreased by more than an order of magnitude when either of the hydroxyl groups was eliminated from the ribose ring. This resulted
Structural organization of chloroplast coupling factor.
Journal:Biochemistry
PubMed ID:2859887
'Fluorescence resonance energy transfer measurements have been used to construct spatial maps for the accessible sulfhydryl of the gamma subunit (dark site) and the essential tyrosine residue of the beta subunits relative to previously mapped sites on the H+-ATPase from chloroplasts. The extent of energy transfer was measured between a