Gel filtration of dilute human embryonic hemoglobins reveals basis for their increased oxygen binding.
Anal Biochem
; 519: 38-41, 2017 Feb 15.
Article
em En
| MEDLINE
| ID: mdl-27965062
ABSTRACT
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.
Palavras-chave
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Oxigênio
/
Hemoglobinas
/
Hemoglobinas Anormais
/
Cromatografia em Gel
/
Embrião de Mamíferos
Limite:
Humans
Idioma:
En
Revista:
Anal Biochem
Ano de publicação:
2017
Tipo de documento:
Article
País de afiliação:
Estados Unidos