Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Raymund F. Eich"'
Autor:
Xuefeng Zhao, K. Vyas, Bao D. Nguyen, Krishnakumar Rajarathnam, Gerd N. La Mar, Tiansheng Li, George N. Phillips, Raymund F. Eich, John S. Olson, Jinshu Ling, David F. Bocian
Publikováno v:
Journal of Biological Chemistry. 270:20763-20774
The functional, spectral, and structural properties of elephant myoglobin and the L29F/H64Q mutant of sperm whale myoglobin have been compared in detail by conventional kinetic techniques, infrared and resonance Raman spectroscopy, 1H NMR, and x-ray
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a70009668244fe92e266b47a46d75450
https://doi.org/10.1074/jbc.270.35.20763
https://doi.org/10.1074/jbc.270.35.20763
Publikováno v:
Biophysical chemistry. 98(1-2)
The ligand binding properties and resistances to denaturation of >300 different site-directed mutants of sperm whale, pig, and human myoglobin have been examined over the past 15 years. This library of recombinant proteins has been used to derive che
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f6297163468ac0845992323be975506
https://pubmed.ncbi.nlm.nih.gov/12128195
https://pubmed.ncbi.nlm.nih.gov/12128195
Publikováno v:
The Journal of biological chemistry. 273(36)
Despite a large amount of work over the past 30 years, there is still no universal agreement on the differential reactivities of the individual alpha and beta subunits in human hemoglobin. To address this question systematically, we prepared a series
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d8daaef1f3c3565ba93d094d639e7194
https://pubmed.ncbi.nlm.nih.gov/9722544
https://pubmed.ncbi.nlm.nih.gov/9722544
Publikováno v:
Artificial cells, blood substitutes, and immobilization biotechnology. 25(1-2)
Over the past five years our laboratory has been using rational, comparative, and random combinatorial mutagenesis strategies to optimize the alpha and beta subunits of recombinant human hemoglobin (Hb) for efficient O2 transport, greater stability,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::61f0e25365c21c2e64bd704675466e6e
https://pubmed.ncbi.nlm.nih.gov/9083641
https://pubmed.ncbi.nlm.nih.gov/9083641
Autor:
Shawn R. Curry, Raymund F. Eich, John S. Olson, Antony J. Mathews, Tiansheng Li, Douglas D. Lemon, Robert D. Smith, Kenneth A. Johnson, Daniel H. Doherty, Jacqueline F. Aitken, George N. Phillips
Publikováno v:
Biochemistry. 35(22)
Nitric oxide (NO) has been implicated as mediator in a variety of physiological functions, including neurotransmission, platelet aggregation, macrophage function, and vasodilation. The consumption of NO by extracellular hemoglobin and subsequent vaso
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8ec7bc58a4abae3af3afced448de4b55
https://pubmed.ncbi.nlm.nih.gov/8679521
https://pubmed.ncbi.nlm.nih.gov/8679521