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. 1971 Mar;68(3):609–613. doi: 10.1073/pnas.68.3.609

Heme Binding and Transport—A Spectrophotometric Study of Plasma Glycoglobulin Hemochromogens

David L Drabkin 1
PMCID: PMC389000  PMID: 4100308

Abstract

A hitherto unreported phenomenon is the immediate production of the spectrum of ferrohemochromogens (in the presence of sodium dithionite) upon the addition in vitro of hydroxyhemin (pH 7.6-7.8) to the plasmas or sera, as well as to certain Cohn plasma protein fractions, of all mammalian species thus far examined. This distinctive reaction is characteristic of a coordination complex with heme iron, and is ascribed to a remarkable affinity for heme of certain plasma glycoglobulins, which include hemopexin. Spectrophotometry has permitted estimations of the specific heme-binding capacity (as ferrohemochromogen) of the plasmas, the rate of removal from plasma of injected heme, and the production of bile pigments therefrom. The study leads to a new proposal of the cooperative roles of the glycoglobulin hemochromogens and hematin-albumin in heme transport and bile pigment production.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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