Heme Binding and Transport—A Spectrophotometric Study of Plasma Glycoglobulin Hemochromogens
AUTOR(ES)
Drabkin, David L.
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=389000Documentos Relacionados
- Spectrophotometric determination of total proteins in blood plasma: a comparative study among dye-binding methods
- Use of heme reporters for studies of cytochrome biosynthesis and heme transport.
- An Improved Spectrophotometric Method To Study the Transport, Attachment, and Breakthrough of Bacteria through Porous Media
- Sulfonamide Resistance of Propionibacteria: Nutrition and Transporta
- A SPECTROPHOTOMETRIC STUDY OF CLASS A STARS