Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Alice De Young"'
Publikováno v:
Proteins: Structure, Function, and Genetics. 39:166-169
As indicated by peptide analyses and mass spectrometry estimations, intramolecular crosslink with bis(3,5-dibromosalicyl)adipate of bovine hemoglobin results in the formation of two main components covalently bridged across the beta-cleft. In one com
Autor:
Michael L. Doyle, Gary K. Ackers, Laurent Kiger, Jo M. Holt, Alexandra L. Klinger, Robert W. Noble, Laura D. Kwiatkowski, Alice De Young
Publikováno v:
Biochemistry. 37:4336-4345
In human hemoglobin (Hb) the beta37 tryptophan residue (betaW37), located at the hinge region of the alpha1beta2 interface, forms many contacts with alpha subunit residues of the opposite dimer, in both the T and R quaternary structures. We have carr
Autor:
Richard L. Haedrich, Robert W. Noble, Lei-Ting Tam, Bonnie J. Davis, Austen Riggs, Laura D. Kwiatkowski, Alice De Young
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 870:552-563
The ligand binding properties of the hemoglobins of several deep-sea, bottom-living fish have been examined. These include five species of rattails (Macrouridae) and Antimora rostrata, all of which possess swimbladders, and two unrelated species with
Autor:
Claudio Dalvit, Massimo Cerdonio, Robert W. Noble, Alice De Young, Gino Mariotto, Aldo Fontana, S. Vitale
Publikováno v:
FEBS Letters. 140:303-306
Autor:
Robert W. Noble, Kasper H. Winterhalter, Stefano Vitale, Ernesto E. Di Iorio, Massimo Cerdonio, Silvia Morante, Alice De Young
Publikováno v:
Scopus-Elsevier
The effective magnetic moments for a number of human and carp methemoglobin derivatives were determined in solution at room temperature. The data permit us to confirm the dependence of the spin-state equilibrium of azide methemoglobin on the quaterna
Publikováno v:
Journal of Biological Chemistry. 247:2493-2498
The pH dependence of the equilibrium and kinetics of ligand binding to carp hemolysate and the purified hemoglobin components of carp hemolysate with O2 and CO has been studied. The affinity of carp hemoglobin for O2 at alkaline pH is 160 times that
Autor:
Alice De Young, Chien Ho, Claudio Dalvit, Massimo Cerdonio, Robert W. Noble, Shigetoshi Miura
Publikováno v:
European journal of biochemistry. 141(2)
The high-resolution proton nuclear magnetic resonance spectra of carp hemoglobin have been compared to those of human normal adult hemoglobin. Carp deoxy and carbonmonoxy hemoglobins in the deoxy-type quaternary state exhibit two downfield exchangeab
Publikováno v:
Scopus-Elsevier
The effects of protein conformation on the spin-state equilibria of several derivatives of carp hemoglobin have been examined. This has been done by measuring the pH dependence of the paramagnetic susceptibilities of these derivatives in the presence
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5f6ee56ec9dd90fcd8e141256eb84899
http://www.scopus.com/inward/record.url?eid=2-s2.0-0023642626&partnerID=MN8TOARS
http://www.scopus.com/inward/record.url?eid=2-s2.0-0023642626&partnerID=MN8TOARS
Autor:
Claudio Dalvit, Robert W. Noble, Irina M. Russu, Stefano Vitale, Alice De Young, Silvia Morante, Chien Ho, Massimo Cerdonio
Publikováno v:
Scopus-Elsevier
We have extended our studies on the magnetic properties of carp carbonmonoxyhemoglobin and the dependence of these properties upon solution variables. Using an improved version of the superconducting magnetometer, we have found that the magnetic susc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::70a82b4a692ce5ec1125c5ad9767148f
http://www.scopus.com/inward/record.url?eid=2-s2.0-0021106028&partnerID=MN8TOARS
http://www.scopus.com/inward/record.url?eid=2-s2.0-0021106028&partnerID=MN8TOARS