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Hydroxide binding equilibrium in hemerythrin

The measurement of the equilibrium constant and the thermodynamic parameters of the binding of hydroxide ions to the active site of hemerythrin, an invertebrate iron containing protein, was done by a new difference spectroscopic method. The method enables accurate measurements of equilibrium constants without accurate knowledge of molar absorptivities or protein concentrations and is novel in that it takes the difference between the two equilibrium mixtures, thus enabling the measurement of equilibrium constants when it is not convenient or possible to produce either substance as a pure reference material.

Identiferoai:union.ndltd.org:pdx.edu/oai:pdxscholar.library.pdx.edu:open_access_etds-4220
Date01 January 1982
CreatorsMcCallum, John David
PublisherPDXScholar
Source SetsPortland State University
Detected LanguageEnglish
Typetext
Formatapplication/pdf
SourceDissertations and Theses

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