Search results for "Hemoglobin binding"
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Isolation of a hemin and hemoglobin binding outer membrane protein of Vibrio vulnificus biotype 2 (serogroup E)
2006
The eel pathogen Vibrio vulnificus biotype 2 (serogroup E) is able to use hemin (Hm) or hemoglobin (Hb) as the sole iron source for growth in vitro and in vivo. The mechanism of heme-iron acquisition in this bacterium requires a direct interaction through binding sites on the bacterial surface (constitutive outer membrane proteins). Using affinity chromatography techniques, a unique protein of around 36.5 kDa was isolated from cell envelopes of E86 strain regardless of the affinity ligand used, hemoglobin or hemin. This protein was purified from both iron-enriched and iron-restricted grown cells. These results support the hypothesis that in this pathogen Hm- and Hb-iron acquisition is media…
The Proton Bohr Factor of Native and Crosslinker Treated Hemoglobins - Its Possible Significance for the Efficacy of Hemoglobin Based Artificial Oxyg…
1994
Especially the (alkaline) proton Bohr effect seems to provide an important self regulating mechanism of the organism to deliver specifically oxygen into tissues suffering from O2 deficit. In this way these tissues switch from aerobic to anaerobic metabolism, get lactacid, thereby shifting oxygen hemoglobin binding curve to the right and thus facilitating the oxygen release. The higher the absolute value of the proton Bohr factor (: delta logP50/ delta pH) is the better this mechanism works. To get one characteristic number the proton Bohr factor at pH 7.1 is taken. This pH in blood is about a lower limit for organism and human blood has at this pH its maximum proton Bohr factor which is abo…