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W R Carper

Publications and source records attributed to W R Carper.

At least 19 recordsLinked to original sources
PubMed2004

A Bloembergen-Purcell-Pound 13C NMR relaxation study of the ionic liquid 1-butyl-3-methylimidazolium hexafluorophosphate.

The molecular structure and rotational motion of the ionic liquid 1-butyl-3-methylimidazolium hexafluorophosphate ([BMIM][PF6]) were studied over a wide temperature range using the Bloembergen-Purcell-Pound 13C NMR spin-lattice relaxation method and NOE factors. Examination of the spin-lattice relaxation times (T1) and the rates (R1 = 1/T1) of the 1-butyl-3-methylimidazolium cation reveals the relative motions of each carbon in the imidazolium cation. The rotational characteristics of the [BMIM] cation are supported by ab-initio molecular structures of [BMIM][PF6] using density functional theory (DFT) and Hartree-Fock (HF) methods. The ab-initio gas phase structures of [BMIM][PF6] indicate that the 1-butyl-3-methylimidazolium C2 hydrogen, the ring methyl group, and the butyl side-chain hydrogen atoms form hydrogen bonds with the hexafluorophosphate anion.

Journal Article↗
PubMed2001

Examination of cadmium(II) complexation by the Suwannee River fulvic acid using 113Cd NMR relaxation measurements.

Aquatic and terrestrial fulvic acids are environmentally important because they affect the bioavailability and transport of metal ions. Prior studies demonstrated that Cd(ll) binds to the oxygen containing functional groups of fulvic acids. The complexation of Cd(II) is further investigated in this study using 113Cd NMR relaxation measurements for solutions of the Suwannee River fulvic acid (SRFA). Spin-lattice (T1) and spin-spin (T2) relaxation times are measured over a range of Cd(II):SRFA ratios. The results clearly indicate two types of Cd(II) binding sites for the SRFA. A series of model ligands was also examined to gain further understanding of the two types of binding motifs present in the fulvic acid. The results for a model compound containing several carboxylate functionalities in near proximity correspond very closely to the results obtained for the strong binding sites of the Cd(II)-SRFA complexes.

Algorithms↗
PubMed2001

Measurement of cadmium(II) and calcium(II) complexation by fulvic acids using 113Cd NMR.

Aquatic and terrestrial fulvic acids are environmentally important in pollution transport because they affect the bioavailability and transport of metal ions. The complexation of the metal ions, Cd(II) and Ca(II), with several fulvic acids is examined in this study using 113Cd NMR. Our results indicate that Cd(II) predominately binds to the oxygen containing functional groups of the fulvic acids. A single 113Cd NMR resonance is observed in NMR spectra of Cd(II)-fulvic acid solutions indicating fast exchange between free and complexed cadmium species. An average association equilibrium constant, K(Cd), is determined from NMR spectra measured for the titration of fulvic acid with Cd(II). The K(Cd) values determined for the four fulvic acids studied range between 1.2 and 3.5 x 10(3) M(-1). Competitive binding between Ca(II) and Cd(II) is used to indirectly determine an average association equilibrium constant, K(Ca), for Ca(II) with each fulvic acid. Overall K(Ca) values range from 4.6 to 7.8 x 10(2) M(-1).

Benzopyrans↗
PubMed1988

Affinity chromatography of glucose dehydrogenase.

Porcine liver beta-D-glucose dehydrogenase, a multi-functional protein, has been purified to apparent homogeneity. The enzyme has been separated from the endoplasmic reticulum using Triton X-114 and further purified using NAD to release glucose dehydrogenase from a NADP-linked sepharose column. The purified enzyme is capable of producing both NADH and NADPH in vivo as indicated by kinetic studies.

Animals↗
PubMed1987

Inhibitory effect of disulfiram (Antabuse) on alcohol dehydrogenase activity.

We investigated the effect of disulfiram (Antabuse) on the activity of alcohol dehydrogenase (EC 1.1.1.1) in vitro. We observed a time-dependent inhibition of this dehydrogenase by disulfiram and diethyldithiocarbamate similar to that obtained for aldehyde dehydrogenase (EC 1.2.1.3). These results suggest a possible explanation for various side effects observed in the clinical use of Antabuse.

Alcohol Dehydrogenase↗
PubMed1983

Characterization studies of glucose dehydrogenase.

Porcine liver beta-D-glucose dehydrogenase has been isolated using Triton X-114 to release it from the endoplasmic reticulum. The purified enzyme contains a limited amount (1.7%) of lipid material, including cholesterol, fatty acids, mono and diglycerides, phosphatidylcholine, phosphatidylethanolamine, and cholesterol esters. This enzyme is a tetrameric protein containing an extensive number of hydrophobic residues. This form of glucose dehydrogenase is capable of turning over both beta-D-glucose and alpha-D-glucose-6-phosphate in vivo as indicated from a steady state kinetic analysis at 37 degrees C.

Amino Acids↗
PubMed1983

Guanidinium- and temperature-induced conformational changes in glucose dehydrogenase.

The conformational changes in glucose dehydrogenase are studied as a function of temperature and guanidinium chloride (GdmCl) concentration. The data were analyzed assuming a two-conformer model which gave similar results using either circular dichroism or enzyme activity. The free energy of denaturation was 0.94 kcal/mol from specific activity and 1.64 kcal/mol from circular dichroism measurements. The mid-point of the denaturation curve was 0.65 or 0.63 M GdmCl, as determined by specific activity or circular dichroism, respectively. The transition temperature, 6.4 degrees C, is close to that of a microsomal membrane phase change, a result that is consistent with the fact that glucose dehydrogenase contains lipid materials when isolated with a non-ionic detergent such as Triton X-114. As the temperature increased, the amount of beta-pleated sheet increased, and the alpha-helical content decreased, suggested that glucose dehydrogenase contains a stable core of beta-pleated sheet.

Animals↗
PubMed1976

6-Phosphogluconate dehydrogenase. Purification and kinetics.

A method is described for the isolation and purification of 6-phosphogluconate dehydrogenase from pig liver. The molecular weight is estimated at 83,000 and that of the subunits is 42,000 as determined by gel electrophoresis. The pH maximum is 8.5 in 50 mM glycine/NaOH buffer and from 7.5 to 10 in 50 mM phosphate buffer at 30 degrees. Magnesium ion is not required for activity and acts as an inhibitor at concentrations above 20 mM. A cellular fractionation study indicates that this enzyme is located almost entirely within the soluble portion of the cytoplasm. Kinetic studies have been done in 50 mM glycine buffer, pH 8.5, at 30 degrees. The data are consistent with a sequential mechanism in which NADP+ is added first, followed by 6-phosphogluconate, and the products are released in the order, CO2, ribulose 5-phosphate, and NADPH. The Michaelis constant is 13.5 muM for 6-phosphogluconate. Dissociation constants are 4.8 muM for NADP+ and 5.1 muM for NADPH.

Animals↗
PubMed1976

Glucose-6-phosphate dehydrogenase. Purification and partial characterization.

Glucose-6-phosphate dehydrogenase has been purified 1000-fold from pig liver. This enzyme exists as an active dimer of molecular weight 133,000 and an inactive monomer of molecular weight 67,500. The pH of maximum activity is 8.5 and the ionic strength maximum is 0.1 to 0.5 M. Glucose-6-phosphate dehydrogenase is highly specific for NADP+ and glucose 6-phosphate. Apparent Km values of 3.6 muM and 5.4 muM were obtained for glucose 6-phosphate and NADP+. This enzyme is located almost entirely within the soluble portion of the cellular cytoplasm.

Animals↗
PubMed1976

A kinetic study of glucose-6-phosphate dehydrogenase.

The steady state kinetics of pig liver glucose-6-phosphate dehydrogenase is consistent with an ordered, sequential mechanism in which NADP is bound first and NADPH released last. Kia is 9.0 muM, Ka is 4.8 muM, and Kb is 36 muM. Glucosamine 6-phosphate, a substrate analogue and competitive inhibitor, is used to help rule out a possible random mechanism. ADP is seen to form a complex with the free form of the enzyme whereas ATP forms a complex with both the free and E-NADP forms of the enzyme. The KI for the E-ADP complex is 1.9 mM, while the Ki values for the E-ATP and E-NADP-ATP complexes are 7.2 and 4.5 mM, respectively.

Adenosine Triphosphate↗