Zobrazeno 1 - 10
of 37
pro vyhledávání: '"William S. Brinigar"'
Publikováno v:
Artificial Cells, Blood Substitutes, and Biotechnology. 35:45-52
This paper describes the approaches we have taken to construct a) mutant hemoglobins with different oxygen affinities, and b) mutant hemoglobins and myoglobins that polymerize to high molecular weight aggregates in an effort to prevent extravasation
Publikováno v:
Transfusion Alternatives in Transfusion Medicine. 5:516-520
SUMMARY Molecular biology offers the opportunity to construct hemoglobin molecules as blood substitutes tailored to specific therapeutic applications. Oxygen affinity can be manipulated by amino acid substitutions in the heme pocket or on the protein
Autor:
Clara Fronticelli, Michael Karavitis, Maria Teresa Sanna, William S. Brinigar, Kevin M. Bobofchak
Publikováno v:
Biophysical Chemistry. 98:115-126
Previous studies on bovine hemoglobin (HbBv) have suggested amino acid substitutions, which might introduce into human hemoglobin (HbA) functional characteristics of HbBv, namely a low intrinsic oxygen affinity regulated by Cl(-). Accordingly, we hav
Autor:
Maurizio Leone, Michael Karavitis, Antonio Cupane, Clara Fronticelli, William S. Brinigar, Gregory B. Vasquez, Valeria Militello
Publikováno v:
Journal of Biological Chemistry. 273:23740-23749
The spectroscopic, conformational, and functional properties of mutant carbonmonoxy hemoglobins in which either the β-globin Val67(E11) or the α-globin Val62(E11) is replaced by threonine have been investigated. The thermal evolution of the Soret a
Autor:
Michael Karavitis, Valeria Militello, Fred K. Friedman, Maurizio Leone, William S. Brinigar, Antonio Cupane, Clara Fronticelli, Gregory B. Vasquez, Aditya P. Koley
Publikováno v:
Journal of Biological Chemistry. 272:26271-26278
The dynamic and functional properties of mutant deoxyhemoglobins in which either the β-globin Val67(E11) or the α-globin Val62(E11) is replaced by threonine have been investigated through the thermal evolution of the Soret absorption band in the te
Autor:
Aditya P. Koley, Clara Fronticelli, Michael Karavitis, Maria Teresa Sanna, Fred K. Friedman, Irina M. Russu, Anna Razynska, William S. Brinigar
Publikováno v:
Journal of Biological Chemistry. 272:3478-3486
The α-globin of human hemoglobin was expressed in Escherichia coli and was refolded with heme in the presence and in the absence of native β-chains. The functional and structural properties of the expressed α-chains were assessed in the isolated s
Autor:
Michael Karavitis, Igor Pechik, Gary L. Gilliland, Krzysztof Fidelis, Clara Fronticelli, William S. Brinigar, Xinhua Ji, John Moult
Publikováno v:
Biochemistry. 35:1935-1945
The crystal structure of the mutant deoxyhemoglobin in which the beta-globin Val67(E11) has been replaced with threonine [Fronticelli et al. (1993) Biochemistry 32, 1235-1242] has been determined at 2.2 A resolution. Prior to the crystal structure de
Autor:
Maria Teresa Sanna, Gabriela C. Perez-Alvarado, A-Lien Lu, Michael Karavitis, Clara Fronticelli, William S. Brinigar
Publikováno v:
Journal of Biological Chemistry. 270:30588-30592
Bovine erythrocytes do not contain 2,3-diphosphoglycerate, the principal allosteric effector of human hemoglobin. Bovine hemoglobin has a lower oxygen affinity than human hemoglobin and is regulated by physiological concentrations of chloride (Fronti
Autor:
Maurizio Leone, Cupane A, William S. Brinigar, Valeria Militello, A-Lien Lu, Clara Fronticelli
Publikováno v:
Proteins: Structure, Function, and Genetics. 22:12-19
The thermal behavior of the Soret band relative to the carbonmonoxy derivatives of some beta-chain mutant hemoglobins is studied in the temperature range 300-10 K and compared to that of wild-type carbonmonoxy hemoglobin. The band profile at various
Autor:
Jeffries L.G. Bucci, Emilia Chiancone, Clara Fronticelli, William S. Brinigar, A-Lien Lu, Maurizio Gattoni
Publikováno v:
Biophysical Chemistry. 51:53-57
The dimer-tetramer association constants of several recombinant human hemoglobins (in the CO form) have been measured by differential gel filtration. Recombinant human hemoglobin prepared from recombinant β-chains, and mutant hemoglobins where the s