Zobrazeno 1 - 10
of 25
pro vyhledávání: '"E.K. Rooney"'
Publikováno v:
Cell Calcium. 16:509-522
Calcium uptake by microsomal membranes from the cellular slime mould Dictyostelium discoideum was measured using Calcium Green-2 as a fluorescent probe of external free Ca 2+ concentration. High-affinity Ca 2+ uptake was found to be completely inhibi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::345b70918c014fd64ba0da82fcc5a4ff
https://doi.org/10.1016/0143-4160(94)90081-7
https://doi.org/10.1016/0143-4160(94)90081-7
Publikováno v:
Biochemistry. 21:6441-6446
The fluorescence emission spectrum of dansylundecanoic acid is sensitive to the environment and appears at a lower wavelength when the fatty acid is bound to protein than when it is bound to phospholipid. When bound to the (Ca2+-Mg2+)-ATPase of sarco
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9b918eac62673d39dac67bfd6fd8b976
https://doi.org/10.1021/bi00268a019
https://doi.org/10.1021/bi00268a019
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 728:159-170
We present a method by which it is possible to describe the binding of fatty acids to phospholipid bilayers. Binding constants for oleic acid and a number of fatty acids used as spectroscopic probes are deduced from electrophoresis measurements. Ther
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::36b5b79549b86b167b056538735b73b9
https://doi.org/10.1016/0005-2736(83)90467-4
https://doi.org/10.1016/0005-2736(83)90467-4
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 732:441-454
We have studied the binding of dansyl propranolol to lipid bilayers and to the (Ca2+ + Mg2+)-ATPase of sarcoplasmic reticulum. The fluorescence emission spectra for dansyl propranolol bound to the ATPase system can be fitted to the sum of three peaks
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::54c00b576cbdc1cf10909c1d6aa62b90
https://doi.org/10.1016/0005-2736(83)90061-5
https://doi.org/10.1016/0005-2736(83)90061-5
Publikováno v:
Biochimica et biophysica acta. 693(2)
Quenching of the fluorescence of the ( Ca 2+ + Mg 2+ )- ATPase purified from muscle sarcoplasmic reticulum can be used to measure relative binding constants of hydrophobic compounds to the phospholipid-protein interface. We show that the binding cons
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::539d8fe511286a8a983af921b501fa8c
https://pubmed.ncbi.nlm.nih.gov/6130787
https://pubmed.ncbi.nlm.nih.gov/6130787
Autor:
Anthony G. Lee, E.K. Rooney
Publikováno v:
Biochimica et biophysica acta. 732(2)
Microelectrophoretic studies of the binding of a number of commonly used hydrophobic amine drugs to liposomes demonstrated the existence of relatively large surface potentials associated with binding of the protonated forms of the drugs. A theoretica
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::96eced91fc558fc55606ed41bf76086d
https://pubmed.ncbi.nlm.nih.gov/6135445
https://pubmed.ncbi.nlm.nih.gov/6135445
Autor:
E.K. Rooney, A.G. Lee
Publikováno v:
Journal of biochemical and biophysical methods. 12(3)
We show that fluorescence emission spectra for molecules containing the dansyl fluorophor can be accurately described as skewed Gaussians, and that spectra for dansyl probes bound to biological membranes can be resolved using least-squares techniques
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ba1e49e449e87b812cd7251310afe24b
https://pubmed.ncbi.nlm.nih.gov/3711585
https://pubmed.ncbi.nlm.nih.gov/3711585
Publikováno v:
Biochemical pharmacology. 28(14)
Interaction between a variety of antihistamines and lipid bilayers has been studied. The H 1 -antagonists all reduce the phase transition temperature of dipalmitoyl phosphatidylcholine, and these data have been used to calculate binding constants for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::55a40e85fc544498d7cc9f7a67a0b300
https://pubmed.ncbi.nlm.nih.gov/40556
https://pubmed.ncbi.nlm.nih.gov/40556
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