Gel filtration of dilute human embryonic hemoglobins reveals basis for their increased oxygen binding.

Autor: Manning LR; Department of Biology, Northeastern University, Boston, MA 02115, USA., Popowicz AM; Information Technology, The Rockefeller University, New York, NY 10065, USA., Padovan JC; Laboratory for Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University, New York, NY 10065, USA., Chait BT; Laboratory for Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University, New York, NY 10065, USA., Manning JM; Department of Biology, Northeastern University, Boston, MA 02115, USA. Electronic address: j.manning@neu.edu.
Jazyk: angličtina
Zdroj: Analytical biochemistry [Anal Biochem] 2017 Feb 15; Vol. 519, pp. 38-41. Date of Electronic Publication: 2016 Dec 11.
DOI: 10.1016/j.ab.2016.12.008
Abstrakt: This report establishes a correlation between two known properties of the human embryonic hemoglobins-- their weak subunit assemblies as demonstrated here by gel filtration at very dilute protein concentrations and their high oxygen affinities and reduced cooperativities reported previously by others but without a mechanistic basis. We demonstrate here that their high oxygen affinities are a consequence of their weak assemblies. Weak vs strong hemoglobin tetramers represent a regulatory mechanism to modulate oxygen binding capacity by altering the equilibrium between the various steps in the assembly process that can be described as an inverse allosteric effect.
Competing Interests: Declaration of Interest The authors report no conflict of interest.
(Copyright © 2016 Elsevier Inc. All rights reserved.)
Databáze: MEDLINE
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