pH dependence of the dissociation of multimeric hemoglobin probed by high hydrostatic pressure

Ferric species equilibrium of the giant extracellular hemoglobin of Glossoscolex paulistus in alkaline medium: HALS hemichrome as a precursor of pentacoordinate species

“…The intense alkaline dissociation of the oligomeric structure of HbGp, around pH 9.0 has been characterized [11,21] and its impact on the polypeptide arrangement is very significant, since the giant extracellular hemoglobin presents an extraordinary mass of 3.6 MDa and its 180 constituent subunits lose their packed assembly upon dissociation. The oligomeric dissociation favors the increase of the water solvent permeability into the heme pocket, originating typical changes in the first coordination sphere of the iron.…”

Effect of High Hydrostatic Pressure on Aeromonas hydrophila AH 191 Growth in Milk

“…The system used consisted of a high‐pressure chamber from ISS Inc. (Champaign, Ill., U.S.A.) and a model HP high pressure cell (Bispo and others 2007) with an internal cavity (diameter: 15 mm; height: 35 mm) in which was placed a cylindrical 1.5 mL quartz cuvette containing the sample to be subjected to high pressure. To avoid contact with the sample fluid that transmits pressure, the cuvette was sealed with a polyethylene tube, the extremity of which was closed at high temperature.…”

Giant Extracellular Hemoglobin of Glossoscolex paulistus: An excellent Prototype of Biosensor and Blood Substitute

“…The hemoglobin (Hb) of the annelid Glossoscolex paulistus is a giant extracellular Hb (erythrocruorin) that dissociates into low affinity subunits after incubation under pressure (with stabilization of the dissociated products), alkalization (mainly around pH 9.0) of acidification of medium or surfactant addition (Bispo et al, 2007).…”