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Adenosine phosphate complexes

Acrylates, reactants to extend a polyamine chain. 63, 143, 144. 14.5. 557 Acrylonitrile, reactant to extend a polyamine chain. 52, 53, 63, 64, 357, 545 A-Acyl protecting groups, 47, 48. 418 Adenosine phosphates, complexation of, 13 Agarose. 757 Albumin, 791... [Pg.873]

Adenosine-5 -monophosphate lanthanide complexes NMR, 3,1104 Adenosine phosphates metal complexes, 2, 977 6, 445 Adenosine 5 -triphosphate... [Pg.78]

Mechanism of Action A thienopyridine derivative that inhibits binding of the enzyme adenosine phosphate (ADP) to its platelet receptor and subsequent ADP-mediated activation of aglycoprotein complex. Therapeutic Effect Inhibits platelet aggregation. Pharmacokinetics ... [Pg.290]

Table 11 Log Formation Constants of Some 1 1 Divalent Metal Complexes of Adenosine Phosphates ... Table 11 Log Formation Constants of Some 1 1 Divalent Metal Complexes of Adenosine Phosphates ...
Fig. 20. The diagram at the top is a schematic view of the active center as deduced from the X-ray data from the protein and several substrate related complexes. Bi, Ri, pi, R2, and B2 indicate the relative positions of the bases, riboses and phosphate of the dinucleotide analog UpcA. Position pi is occupied by S(V in the protein crystal. CMP, UMP, and analogs of these occupy Bi, Ri, and pi predominantly. 5 -AMP occupy Bj, Ra, and pi while 3 -AMP and 3 5 -A > p occupy Ba and R2 predominantly, and possibly to a lesser extent, Bi and Ri. B2 is the probable position of the second pyrimidine in dinucleotides such as CpU. The phosphate position in C > p cannot be observed owing to digestion but would be at pi if the base occupies the same position as in CMP. Four His 119 positions are indicated. I coincided with Pi but is a possible position in the absence of S(V or nucleotides. II is behind III and may be occupied by solvent. Ill is slightly stabilized by 3 -CMP. IV is the position occupied when B2 and It2 are occupied by adenosine phosphates. His 12 is behind pi and Ri. There is a solvent molecule, presumably water, behind p, as indicated by H20. Lys 41 enters from the upper right and is not in contact with pi but might contact pi. Asp 121 enters from... Fig. 20. The diagram at the top is a schematic view of the active center as deduced from the X-ray data from the protein and several substrate related complexes. Bi, Ri, pi, R2, and B2 indicate the relative positions of the bases, riboses and phosphate of the dinucleotide analog UpcA. Position pi is occupied by S(V in the protein crystal. CMP, UMP, and analogs of these occupy Bi, Ri, and pi predominantly. 5 -AMP occupy Bj, Ra, and pi while 3 -AMP and 3 5 -A > p occupy Ba and R2 predominantly, and possibly to a lesser extent, Bi and Ri. B2 is the probable position of the second pyrimidine in dinucleotides such as CpU. The phosphate position in C > p cannot be observed owing to digestion but would be at pi if the base occupies the same position as in CMP. Four His 119 positions are indicated. I coincided with Pi but is a possible position in the absence of S(V or nucleotides. II is behind III and may be occupied by solvent. Ill is slightly stabilized by 3 -CMP. IV is the position occupied when B2 and It2 are occupied by adenosine phosphates. His 12 is behind pi and Ri. There is a solvent molecule, presumably water, behind p, as indicated by H20. Lys 41 enters from the upper right and is not in contact with pi but might contact pi. Asp 121 enters from...
R. N. Smith and R. A. Alberty, The apparent stability constants of ionic complexes of various adenosine phosphates and divalent cations, J. Am. Chem. Soc., 78. 2376-2380 (1956). [Pg.190]

A tetraamidinium functionalized, bowl-type cavitand (receptor 8) was developed by Diederich and Sebo [47]. This receptor was found to complex 1,3-dicarboxylate anions with good selectivity and a 1 2 binding stoichiometry both in CD3OD and D20, as revealed by standard Job plot analysis. In contrast, various nucleotide phosphates were found to be bound with a 1 1 stoichiometry in D20. In the case of the adenosine phosphates, the association constants increased as a function of nucleotide charge [i.e., the affinity order (K., M-1) was cAMP (1400) < AMP (10000)charged receptor (8) also showed moderate selectivity towards AMP (Ka = 10 000 M-1) over other nucleotide monophosphate anions, such as GMP (FCa = 5200 M-1), CMP (fCa = 3500 M-1), TMP (K l — 5900 M ), and UMP (Ka-3800M ) in D20 containing TRIS buffer (2.5 mM, pH 8.3). [Pg.322]

Flavin mononucleotide (FMN)-adenosine and flavin adenine dinucleotide (FAD)-adenosine complexes show quenched triplet lifetimes compared to FMN alone, which is cited as evidence of intramolecular com-plexation between the flavins and adenosine by Shiga and Piette [142]. Adenosine phosphates also form complexes with FAD [143]. The com-plexation between a flavin and adenosine is identical to the intermolecular complexing of adenosine and flavin moieties, in the latter case enforced by hydrophobic bonding [144-146]. Rath and McCormick [147] have examined the riboflavin complexes of a series of purine ribose derivatives... [Pg.713]

Early investigations (30) of the rate of internal transesterification of the 4-nitrophenylphosphate ester of propylene glycol (HPNP) and also on RNA oligomers of adenosine phosphate were carried out using Ln(III) complexes of Hgands 13 (32) 14 (32) ind 15 (29, 33, 34). [Pg.302]

Toropov, A.A. and Toropova, A.P. (2001c) QSPR modeling of stability of complexes of adenosine phosphate derivatives with metals absent from the complexes of the teaching access. Russ. J. Coord. Chem., 27, 574-578. [Pg.1185]

Irradiation of water leads to formation of (HO) . By contrast, in the brain, strong water-soluble electron donors (DH) such as nicotinamide adenine dinucleotide phosphate (NADPH), catechin, hydroquinone, ascorbic acid or glutathione (L-y-glutamyl-L-cysteinyl-glycine GSH) can promote formation of (HO) from H2O2 in the presence of Cu+ or some iron complexes (e.g. Fe -adenosine diphosphate complexes) according to Eqs. (15) and (16) (Florence, 1984 Kadiiska et al., 1992). [Pg.441]

The basis of the catalysis of the splitting of the disulfide is presumably the formation of a charge-transfer complex between the two-electron donor NADPH (equivalent to a hydride anion) and the acceptor flavin combined with proximity effects. Both coenzymes, NADPH and FAD, are bound to the protein by adenosine phosphate-protein interactions, the substrate is loosely bound at the cleft between the units of a protein dimer (Fig. 9.6.12) (Schulz, 1983 Douglas, 1987). [Pg.516]

The use of the phosphoenol pyruvate (PEP)/pyruvate kinase system is probably the most useful method for the regeneration of nucleoside triphosphates [523]. PEP is not only very stable towards spontaneous hydrolysis but it is also a stronger phosphorylating agent than ATP. Furthermore, nucleosides other than adenosine phosphates are also accepted by pyruvate kinase. The drawbacks of this system are the more complex synthesis of PEP [524, 525] and the fact that pyruvate kinase is inhibited by pyruvate at higher concentrations. [Pg.114]

Thioanalogues of adenosine phosphates have been studied by n.m.r. and the chemical shifts were compared to those of the oxygenated compounds. The effects of changing pH and the concentration of added Mg + led to the conclusion that chemical shift data cannot yield unequivocal information concerning the absolute structure of the metal complexes of nucleosides but can be used to monitor changes in chelation, for example, in binding to enzymes. ... [Pg.197]

Ill these simultaneous reactions, die energy released when the complex molecule AB is broken down is immediately used to build a molecule of adenosine triphosphate (ATP) from a molecule of adenosine diphosphate (ADP) and an inorganic phosphate (P,). ATP is a high energy compound. It is called the energy currency of the body because once it is formed, it provides energy that the body can spend later to drive vital reactions in cells (Figure 1). [Pg.168]

ADP (adenosine diphosphate) and ATP (adenosine triphosphate) are complex organic molecules (Fig. 17.9) that, in essence, differ only hy the presence of an extra phosphate group in ATP. In the coupled reaction with glucose, about 38 mol of ATP are synthesized for every mole of glucose consumed. This gives an overall free energy change for the coupled reaction of... [Pg.469]


See other pages where Adenosine phosphate complexes is mentioned: [Pg.257]    [Pg.1280]    [Pg.1297]    [Pg.977]    [Pg.1068]    [Pg.49]    [Pg.714]    [Pg.257]    [Pg.666]    [Pg.648]    [Pg.185]    [Pg.369]    [Pg.162]    [Pg.1623]    [Pg.1714]    [Pg.7177]    [Pg.336]    [Pg.447]    [Pg.84]    [Pg.296]    [Pg.398]    [Pg.385]    [Pg.122]    [Pg.125]    [Pg.808]   
See also in sourсe #XX -- [ Pg.369 ]




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Adenosine diphosphate phosphate complex

Adenosine phosphate metal complexes

Adenosine, complexes

Adenosine-5’-phosphat

Phosphate Complexes

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