Výsledky vyhledávání - "L. D. Faller"

Feasibility of analysing [13 C]urea breath tests for Helicobacter pylori by gas chromatography-mass spectrometry in the selected ion monitoring mode

Autor: H. Ajie, L. D. Faller, Dennis M. Jensen, V. N. Kasho, W.-N. P. Lee, S. Cheng

Publikováno v: Alimentary Pharmacology & Therapeutics. 10:985-995

Background: The [13C]urea breath test for Helicobacter pylori is nonradioactive, as well as noninvasive, but few clinical laboratories have the expensive isotope ratio mass spectrometer used for analysis. Methods: To demonstrate the feasibility of an

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::108a866db043967179d06ab6418d620a
https://doi.org/10.1046/j.1365-2036.1996.99271000.x

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18O-exchange evidence that mutations of arginine in a signature sequence for P-type pumps affect inorganic phosphate binding

Autor: R A, Farley, E, Elquza, J, Müller-Ehmsen, D J, Kane, A K, Nagy, V N, Kasho, L D, Faller

Publikováno v: Biochemistry. 40(21)

We have proposed a model for part of the catalytic site of P-type pumps in which arginine in a signature sequence functions like lysine in P-loop-containing enzymes that catalyze adenosine 5'-triphosphate hydrolysis [Smirnova, I. N., Kasho, V. N., an

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::1369266ef13f4bd3b8a87a7e88cd806c
https://pubmed.ncbi.nlm.nih.gov/11371198

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Estimation of the distance change between cysteine-457 and the nucleotide binding site when sodium pump changes conformation from E1 to E2 by fluorescence energy transfer measurements

Autor: S H, Lin, L D, Faller

Publikováno v: Biochemistry. 35(25)

The first indication of the size of a conformational change implicated in ion transport by sodium pump has been obtained by measuring the change in efficiency of fluorescence energy transfer between two specific locations on the alpha-subunit. The do

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::870e54f8f50f20b7523dfceffd5f886b
https://pubmed.ncbi.nlm.nih.gov/8679600

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Mechanism of K+ interaction with fluorescein 5'-isothiocyanate-modified Na+,K(+)-ATPase

Autor: I N, Smirnova, L D, Faller

Publikováno v: The Journal of biological chemistry. 268(22)

The rate of K+ binding to fluorescein 5'-isothiocyanate-modified Na+,K(+)-ATPase has been measured by stopped-flow fluorometry and shown to depend sigmoidally on potassium concentration. By assuming two K+ ions must bind to cause a rate-limiting conf

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::b28d62a66114bf384c0a9df7d7d2d67d
https://pubmed.ncbi.nlm.nih.gov/8393855

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Role of Mg2+ ions in the conformational change reported by fluorescein 5'-isothiocyanate modification of Na+,K(+)-ATPase

Autor: I N, Smirnova, L D, Faller

Publikováno v: Biochemistry. 32(23)

The role of Mg2+ in the conformational change reported by fluorescein 5'-isothiocyanate modification of Na,K-ATPase has been studied by stopped-flow fluorometry. K+ causes a fluorescence quench that is reversed by Na+. The principal experimental obse

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::778ed52dc495007b4b3d7fad11f7c2f4
https://pubmed.ncbi.nlm.nih.gov/8389584

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Temperature dependence of the rates of conformational changes reported by fluorescein 5'-isothiocyanate modification of H+,K(+)- and Na+,K(+)-ATPases

Autor: L D, Faller, R A, Diaz, G, Scheiner-Bobis, R A, Farley

Publikováno v: Biochemistry. 30(14)

Stopped-flow fluorometry has been used to measure the forward and reverse rates of the conformational change from E1 to E2 in the fluorescein-modified proton and sodium pumps (1) as a function of Na+ and K+ concentrations to verify the proposed mecha

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::1e0e3dce56aecf0d38b7f0aae1b0257c
https://pubmed.ncbi.nlm.nih.gov/1849428

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Evidence from 18O exchange measurements for steps involving a weak acid and a slow chemical transformation in the mechanism of phosphorylation of the gastric H+, K+-ATPase by inorganic phosphate

Autor: L D, Faller, R A, Diaz

Publikováno v: Biochemistry. 28(17)

Phosphorylation of the gastric H,K-ATPase by Pi has been studied by measuring the P18Oj16O4-j distribution as a function of time at different H+, K+, and [18O]Pi concentrations. The advantage of isotope exchange measurements is that the P18Oj16O4-j d

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::8a9f7d1bf121dd042fe5e377f3da1d3e
https://pubmed.ncbi.nlm.nih.gov/2554958

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Vanadate binding to the gastric H,K-ATPase and inhibition of the enzyme's catalytic and transport activities

Autor: L D, Faller, E, Rabon, G, Sachs

Publikováno v: Biochemistry. 22(20)

Vanadate inhibition of the catalytic and transport activities of the gastric magnesium-dependent, hydrogen ion transporting, and potassium-stimulated adenosinetriphosphatase (EC 3.6.1.3) (H,K-ATPase) has been studied. The principal experiment observa

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::4005b765cea95aa13ea851cc2e8edd25
https://pubmed.ncbi.nlm.nih.gov/6138094

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The amino acid sequence of an active site peptide from the H,K-ATPase of gastric mucosa

Autor: R A, Farley, L D, Faller

Publikováno v: The Journal of biological chemistry. 260(7)

The gastric H,K-ATPase is an active transport protein that is responsible for the maintenance of a large pH gradient across the secretory canaliculus of the mammalian parietal cell. Acid secretion across these epithelial cell membranes is coupled to

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::2d1691491ffd49d973280782e8d69566
https://pubmed.ncbi.nlm.nih.gov/2984187

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