Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Gerald Godette"'
Publikováno v:
The Journal of biological chemistry. 280(49)
Expression of alpha and beta chains and their post-translational assembly into alpha(2)beta(2) tetramers is fundamental to the formation and function of most vertebrate hemoglobins. There is a strong evolutionary bias that favors expression of equal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d7ffe8f4f35ca778e2e699fb632c6786
https://pubmed.ncbi.nlm.nih.gov/16166086
https://pubmed.ncbi.nlm.nih.gov/16166086
Autor:
Shirley Tesh, Giulia Ferruzzi, Robert W. Henkens, Gerald Godette, Celia Bonaventura, Robert Stevens
Publikováno v:
Biophysical chemistry. 98(1-2)
Factors which govern transnitrosation reactions between hemoglobin (Hb) and low molecular weight thiols may define the extent to which S-nitrosated Hb (SNO-Hb) plays a role in NO in the control of blood pressure and other NO-dependent reactions. We s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8f18afe54cf6cf5354ceb9982286fb69
https://pubmed.ncbi.nlm.nih.gov/12128197
https://pubmed.ncbi.nlm.nih.gov/12128197
Autor:
Linda L. Pearce, David E. Holm, Celia Bonaventura, Jim Peterson, Shirley Tesh, Alvin L. Crumbliss, Joseph Bonaventura, Gerald Godette
Publikováno v:
The Journal of biological chemistry. 274(9)
Previous studies showed that CO/H2O oxidation provides electrons to drive the reduction of oxidized hemoglobin (metHb). We report here that Cu(II) addition accelerates the rate of metHb beta chain reduction by CO by a factor of about 1000. A mechanis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::556164cca188a67081687256acf5700e
https://pubmed.ncbi.nlm.nih.gov/10026163
https://pubmed.ncbi.nlm.nih.gov/10026163
Autor:
M. David Boatright, David E. Holm, Celia Bonaventura, Jim Peterson, Linda L. Pearce, Joseph Bonaventura, Gerald Godette
Publikováno v:
Comparative biochemistry and physiology. Part B, Biochemistrymolecular biology. 114(4)
Contrary to previous reports, the functional and spectral properties of "monomeric" shark cytochrome c oxidases are not entirely similar to those of the "dimeric" beef enzyme. Most significantly, unlike the behavior of beef oxidase, the fully oxidize
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::21390407b2f3cb7db5ec0f0b532f99e6
https://pubmed.ncbi.nlm.nih.gov/8840511
https://pubmed.ncbi.nlm.nih.gov/8840511
Autor:
Claudio Rubiliani, Gerald Godette
Publikováno v:
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry. 70:415-419
1. 1. The incorporation of 3H-Leucine into the CNS of healthy and parasitized Carcinus with Sacculina shows that the protein synthesis and release in the brain and ventral ganglionic mass, and the transfer of material to the eyestalks are reduced int
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b0f863e0d1d403b13e8ed75b305e340b
https://doi.org/10.1016/0305-0491(81)90275-3
https://doi.org/10.1016/0305-0491(81)90275-3
Publikováno v:
Journal of Biological Chemistry. 251:7644-7648
The high molecular weight hemocyanin found in the hemolymph of the horseshoe crab, Limulus polyphemus, is composed of at least eight different kinds of subunits. Ion exchange chromatography at high pH in the presence of EDTA yields five major zones,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::49e270d92f684209005ea36fd086d81c
https://doi.org/10.1016/s0021-9258(17)32900-9
https://doi.org/10.1016/s0021-9258(17)32900-9
Publikováno v:
Journal of Biological Chemistry. 250:9250-9255
Hemoglobin Deer Lodge is an abnormal human hemoglobin with arginine substituted for histidine at the beta 2 position. X-ray crystallography of normal human hemoglobin has shown that the beta 2 residue is normally part of the binding site for 2,3-diph
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a09b7ef4eb95f46d374c74d35ff255a
https://doi.org/10.1016/s0021-9258(19)40636-4
https://doi.org/10.1016/s0021-9258(19)40636-4
Publikováno v:
FEBS Letters. (1-2):53-58
The electronic spectra of fully oxidized derivatives of some cytochrome c oxidase preparations are distinctly pH dependent. In general, the observed spectral shifts are greater in the case of pulsed derivatives compared to resting preparations and al
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5afeb037b2d9c140d7e3dbbef5fe91ab