Coboglobins: Heterotropic Linkage and the Existence of a Quaternary Structure Change Upon Oxygenation of Cobaltohemoglobin

Cobaltohemoglobin prepared from horse hemoglobin retains the full heterotropic linkage properties of the normal iron hemoglobin, including both the Bohr and phosphate effects. From this result, and the known connection between heterotropic linkage properties and hemoglobin conformational change, it...

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Detalhes bibliográficos

Publicado no:	Proc Natl Acad Sci U S A
Principais autores:	Hsu, G. C., Spilburg, C. A., Bull, C., Hoffman, B. M.
Formato:	Artigo
Idioma:	Inglês
Publicado em:	National Academy of Sciences 1972
Assuntos:	Biological Sciences: Biochemistry
Acesso em linha:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC426882/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/4506082/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.69.8.2122
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