Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Ted R. Lindstrom"'
Autor:
Ted R. Lindstrom, Thomas H. Parliment
Publikováno v:
Thermally Generated Flavors ISBN: 9780841227422
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4b13cd0b5174ff7eef6a42cd6e32026b
https://doi.org/10.1021/bk-1994-0543.ch035
https://doi.org/10.1021/bk-1994-0543.ch035
Autor:
Ted R Lindstrom, Seymour H. Koenig
Publikováno v:
Journal of Magnetic Resonance (1969). 15:344-353
The spin-lattice relaxation rates of solvent water protons in solutions of normal and sickle cell hemoglobin, normal red blood cells, and whole blood have been measured at magnetic fields between 5 Oe and 12 kOe. The field-dependent data have been an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::94a77aded32d82202db6eacad70114ac
https://doi.org/10.1016/0022-2364(74)90088-2
https://doi.org/10.1016/0022-2364(74)90088-2
Publikováno v:
Biochemical and Biophysical Research Communications. 45:22-26
When deoxyhemoglobin is titrated with n-butyl isocyanide in the presence of inositol hexaphosphate at pD 7.1, the intensity of the heme proton resonance positioned at ∼-18 ppm downfield from HDO decreases more rapidly than that at ∼-12 ppm. The l
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c9f7813a6edbc42a7344298073886433
https://doi.org/10.1016/0006-291x(71)90044-1
https://doi.org/10.1016/0006-291x(71)90044-1
Autor:
Raymond C. Fort, Ted R. Lindstrom
Publikováno v:
The Journal of Physical Chemistry. 75:3963-3966
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1aeb0b9ae3b8aec6c83030b053de097a
https://doi.org/10.1021/j100695a008
https://doi.org/10.1021/j100695a008
Autor:
Ted R. Lindstrom, Chien Ho
Publikováno v:
Proceedings of the National Academy of Sciences. 69:1707-1710
Nuclear magnetic resonance studies of the contact-shifted spectra of heme protons in deoxyhemoglobin A from human adults show conclusively that oxygen binds to the α hemes in preference to the β hemes. The preferential binding is produced in 10% he
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7d6c57ad61a9569b22d501e55c541df3
https://doi.org/10.1073/pnas.69.7.1707
https://doi.org/10.1073/pnas.69.7.1707
Autor:
Donald G. Davis, Joseph J. Baldassare, Nancy H. Mock, Ted R. Lindstrom, Chien Ho, Richard T. Jones, Samuel Charache
Publikováno v:
Journal of Molecular Biology. 60:101-111
The proton nuclear magnetic resonance spectra of human adult deoxyhemoglobin and several mutant or modified deoxyhemoglobins taken in 0.1 m -deuterated sodium phosphate at pD 7 and 25 °C show three prominent hyperfine shifted lines at approximately
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c0d9e692816269d42a71511d6b50ad89
https://doi.org/10.1016/0022-2836(71)90450-5
https://doi.org/10.1016/0022-2836(71)90450-5
Publikováno v:
Biochemistry. 16(7)
Hemoglobin M Milwaukee (beta67E11 Val leads to Glu) is a naturally occurring valency hybrid containing two permanently oxidized hemes on the beta chains. In this mutant, the two abnormal beta chains cannot combine with ligands whereas the two alpha c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d64c364fbe3ffb5e9b4f3e5afe14d94
https://pubmed.ncbi.nlm.nih.gov/849426
https://pubmed.ncbi.nlm.nih.gov/849426
Publikováno v:
Nature: New biology. 237(78)
Analysis of the NMR spectra of haemoglobin M Milwaukee confirms that ligand binding to the α haems changes the quaternary structure.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4a78d7882c3cb72de5dfb36657ddeac1
https://pubmed.ncbi.nlm.nih.gov/4504457
https://pubmed.ncbi.nlm.nih.gov/4504457
Publikováno v:
Annals of the New York Academy of Sciences. 222
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f9a909d2361b0ed4a8b15178b4979a4
https://pubmed.ncbi.nlm.nih.gov/4361855
https://pubmed.ncbi.nlm.nih.gov/4361855