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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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Bibliografische gegevens
Hoofdauteurs: Hsu, G. C., Spilburg, C. A., Bull, C., Hoffman, B. M.
Formaat: Artigo
Taal:Inglês
Gepubliceerd in: 1972
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Online toegang:https://ncbi.nlm.nih.gov/pmc/articles/PMC426882/
https://ncbi.nlm.nih.gov/pubmed/4506082
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