Comparison Of ATP Research Articles

7-168 - Comparison of ATP, Colony Count and Surface Marker as a Measure of Environmental Cleaning Compliance for Intensive Care Discharge Rooms

7-168 - Comparison of ATP, Colony Count and Surface Marker as a Measure of Environmental Cleaning Compliance for Intensive Care Discharge Rooms

A Computational Approach towards the Understanding of Plasmodium falciparum Multidrug Resistance Protein 1

The emergence of drug resistance in Plasmodium falciparum tremendously affected the chemotherapy worldwide while the intense distribution of chloroquine-resistant strains in most of the endemic areas added more complications in the treatment of malaria. The situation has even worsened by the lack of molecular mechanism to understand the resistance conferred by Plasmodia species. Recent studies have suggested the association of antimalarial resistance with P. falciparum multidrug resistance protein 1 (PfMDR1), an ATP-binding cassette (ABC) transporter and a homologue of human P-glycoprotein 1 (P-gp1). The present study deals about the development of PfMDR1 computational model and the model of substrate transport across PfMDR1 with insights derived from conformations relative to inward- and outward-facing topologies that switch on/off the transportation system. Comparison of ATP docked positions and its structural motif binding properties were found to be similar among other ATPases, and thereby contributes to NBD domains dimerization, a unique structural agreement noticed in Mus musculus Pgp and Escherichia coli MDR transporter homolog (MsbA). The interaction of leading antimalarials and phytochemicals within the active pocket of both wild-type and mutant-type PfMDR1 demonstrated the mode of binding and provided insights of less binding affinity thereby contributing to parasite's resistance mechanism.

Crystallographic Snapshots along the Reaction Pathway of Nucleoside Triphosphate Diphosphohydrolases

In vertebrates, membrane-bound ecto-nucleoside triphosphate diphosphohydrolases (NTPDases) on the cell surface are responsible for signal conversion and termination in purinergic signaling by extracellular nucleotides. Here we present apo and complex structures of the rat NTPDase2 extracellular domain and Legionella pneumophila NTPDase1, including a high-resolution structure with a transition-state analog. Comparison of ATP and ADP binding modes shows how NTPDases engage the same catalytic sitefor hydrolysis of nucleoside triphosphates and diphosphates. We find that this dual specificity is achieved at the expense of base specificity. Structural and mutational studies indicate that a conserved active-site water is replaced by the phosphate product immediately after phosphoryl transfer. Partial base specificity for purines in LpNTPDase1 is based on a different intersubunit base binding site for pyrimidine bases. A comparison of the bacterial enzyme in six independent crystal forms shows that NTPDases can undergo a domain closure motion of at least 17°.

Differential regulation of vacuolar H+-ATPase and H+-PPase in Cucumis sativus roots by zinc and nickel

Zinc and nickel, as micronutrients, are essential for all organisms. We investigated the effect of 10 and 100μM Zn and Ni on two tonoplast proton pumps, vacuolar H+-ATPase (V-ATPase) (EC 3.6.3.14) and vacuolar H+-pyrophosphatase (V-PPase) (EC 3.6.1.1), in cucumber roots. ATP-dependent proton transport as well as ATP hydrolysis, catalyzed by V-ATPase, decreased in roots after exposure of plants to both Zn and Ni under all the examined conditions. In contrast, V-PPase activities, measured as PPi hydrolysis and PPi-driven H+ transport, were stimulated by lower concentration of metals. However, at higher metal concentration, hydrolytic activity of V-PPase remained unchanged, while PPi-dependent proton pumping into the tonoplast vesicles was reduced. When heavy metals were introduced into the enzyme reaction medium, both V-ATPase and V-PPase activities were lowered by Zn and Ni in a similar manner. As the gene expression and immunoblot analyses depicted, observed changes in the activity of both tonoplast proton pumps in response to zinc and nickel were not due to the modification in the expression of the CsVHA-A, CsVHA-c and CsVP genes encoding V-ATPase subunit A and c, and V-PPase, respectively, in cucumber roots or in amounts of enzyme proteins. Moreover, Zn as well as Ni ions did not enhance the lipid peroxidation in the root tonoplast fractions. Comparison of ATP and pyrophosphate contents in the control roots and roots treated with heavy metals revealed that Zn and Ni do not affect the ATP amount but reduce the PPi level.

Comparison of ATP and Ergosterol as Indicators of Fungal Biomass Associated with Decomposing Leaves in Streams

ATP and ergosterol were compared as indicators of fungal biomass associated with leaves decomposing in laboratory microcosms and streams. In all studies, the sporulation rates of the fungi colonizing leaves were also determined to compare patterns of fungal reproductive activity with patterns of mycelial growth. During leaf degradation, ATP concentrations exhibited significant, positive correlations with ergosterol concentrations in the laboratory and when leaves had been air dried prior to being submerged in a stream. However, when freshly shed leaves were submerged in a stream, concentrations of ATP and ergosterol were negatively correlated during degradation. This appeared to be due to the persistence of leaf-derived ATP in freshly shed leaves during the first 1 to 2 weeks in the stream. Estimates of fungal biomass from ergosterol concentrations of leaf litter were one to three times those calculated from ATP concentrations. ATP, ergosterol, and sporulation data generally provided similar information about the fungi associated with decomposing leaves in streams during periods when fungi were growing. Ergosterol concentrations provide a more accurate indication of fungal biomass in situations in which other organisms make significant contributions to ATP pools.

Comparison of ATP and creatine phosphate (CrP) preservation during continuous perfusion of donor hearts with bretschneider, NIH, or UW-cardioplegic solution: A study in the rat: J.Minten, W.Flameng, K.U.Leuven Lab. Exp. Cardiac Surgery, Leuven, Belgium

Comparison of ATP and creatine phosphate (CrP) preservation during continuous perfusion of donor hearts with bretschneider, NIH, or UW-cardioplegic solution: A study in the rat: J.Minten, W.Flameng, K.U.Leuven Lab. Exp. Cardiac Surgery, Leuven, Belgium