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Monodisperse 130 kDa and 260 kDa Recombinant Human Hemoglobin Polymers as Scaffolds for Protein Engineering of Hemoglobin-Based Oxygen Carriers

التفاصيل البيبلوغرافية
العنوان: Monodisperse 130 kDa and 260 kDa Recombinant Human Hemoglobin Polymers as Scaffolds for Protein Engineering of Hemoglobin-Based Oxygen Carriers
المؤلفون: Jacqueline F. Aitken, Spencer J. Anthony-Cahill, Douglas D. Lemon, Michael P. Doyle, David A. Marquardt, Jeffrey S. Davidson, Janet K. Epp
المصدر: Journal of Functional Biomaterials, Vol 3, Iss 1, Pp 61-78 (2012)
بيانات النشر: MDPI AG, 2012.
سنة النشر: 2012
المجموعة: LCC:Biotechnology
LCC:Medicine (General)
مصطلحات موضوعية: polyhemoglobin, dihemoglobin, tetrahemoglobin, hemoglobin engineering, extravasation, pressor response, Biotechnology, TP248.13-248.65, Medicine (General), R5-920
الوصف: 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, and analytical ultracentrifugation. The observed values of P50 and nmax for the dihemoglobin are slightly lower than those observed for the recombinant hemoglobin rHb1.1 (a “monohemoglobin” comprised of two β globins and an αI-Gly-αII diα-globin chain). Titration of the deoxy form of dihemoglobin with CO shows that all eight heme centers bind ligand. In vivo, dihemoglobin showed increased circulating halflife and a reduced pressor response in conscious rats when compared to rHb1.1. These observations suggest that dihemoglobin is an oxygen carrying molecule with desirable in vivo properties and provides a platform for an isooncotic hemoglobin solution derived solely from a recombinant source. A 260 kDa tetrahemoglobin has also been produced by chemical crosslinking of a dihemoglobin that contains a Lys16Cys mutation in the C-terminal α-globin subunit. Tetrahemoglobin also shows reduced vasoactivity in conscious rats that is comparable to that observed for dihemoglobin.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 2079-4983
Relation: http://www.mdpi.com/2079-4983/3/1/61/; https://doaj.org/toc/2079-4983
DOI: 10.3390/jfb3010061
URL الوصول: https://doaj.org/article/b6b0f95ce22843058a5eaa16856d7271
رقم الأكسشن: edsdoj.b6b0f95ce22843058a5eaa16856d7271
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:20794983
DOI:10.3390/jfb3010061