Rational Mutagenesis to Engineer Heme Stability in Recombinant Human Hemoglobin to Design Potential Hemoglobin Based Oxygen Carrier
نویسندگان
چکیده
منابع مشابه
Hemoglobin-based oxygen carriers
Transfusable fluids that may be used as alternatives to red blood cell transfusion offer the promise of preserving tissue perfusion and minimizing hypoxic cellular damage, and this promise may soon be fulfilled. Clinical testing of hemoglobin-based oxygen carriers has faced and met challenges involving molecular design, safety, efficacy, and regulatory requirements. Three leading candidates hav...
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The effects of electromagnetic fields (EMFs) radiation at the frequency of 940 MHz on the structure and function of human adult and fetal hemoglobin (HbA and HbF) were studied. After extraction and purification of HbA and HbF, the oxygen absorption values for exposed and unexposed HbA and HbF to EMF were compared. The slope of oxygen absorption curve for exposed HbA was increased while that for...
متن کاملMonodisperse 130 kDa and 260 kDa Recombinant Human Hemoglobin Polymers as Scaffolds for Protein Engineering of Hemoglobin-Based Oxygen Carriers
A recombinant 130 kDa dihemoglobin which is made up of a single-chain tetra-α globin and four β globins has been expressed as a soluble protein in E. coli. The sequence of the single chain tetra-α is: αI-Gly-αII-(SerGlyGly)5Ser-αIII-Gly-αIV. This dihemoglobin has been purified and characterized in vitro by size exclusion chromatography, electrospray mass spectroscopy, equilibrium oxygen binding...
متن کاملEndothelial dysfunction enhances vasoconstriction due to scavenging of nitric oxide by a hemoglobin-based oxygen carrier.
BACKGROUND To date, there is no safe and effective hemoglobin-based oxygen carrier (HBOC) to substitute for erythrocyte transfusion. It is uncertain whether a deficiency of endothelial nitric oxide bioavailability (endothelial dysfunction) prevents or augments HBOC-induced vasoconstriction. METHODS Hemodynamic effects of infusion of PolyHeme (1.08 g hemoglobin/kg; Northfield Laboratories, Eva...
متن کاملA human hemoglobin with lowered oxygen affinity and impaired heme-heme interactions.
The reactivity of the iron in the four hemes of the mammalian hemoglobin molecule depends largely on the interactions between the prosthetic groups and the amino acid chains of the globin (1, 2). Normal configuration of heme groups in the abnormal human hemoglobins, therefore, does not preclude anomalies of their oxygen affinity which might arise from aberrations in the globin. In most of the m...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2020
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2019.11.2817