Haem degradation in abnormal haemoglobins
- 1 September 1978
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 173 (3), 985-987
- https://doi.org/10.1042/bj1730985
Abstract
The coupled oxidation of certain [human] abnormal Hb led to different bile-pigment isomer distributions from that of normal Hb. The isomer pattern may be correlated with the structure of the abnormal Hb in the neighborhood of the heme pocket. This is support for heme degradation by an intramolecular reaction.This publication has 10 references indexed in Scilit:
- Stereospecific haem cleavage. A model for the formation of bile-pigment isomers in vivo and in vitroBiochemical Journal, 1976
- STRUCTURE AND MECHANISM OF HAEMOGLOBINBritish Medical Bulletin, 1976
- THE ENZYMATIC FORMATION OF BILIRUBIN*Annals of the New York Academy of Sciences, 1975
- Haemoglobulin catabolism: the role of ferrihaems in studies of the degradation pathway (Short Communication)Biochemical Journal, 1974
- The meso-reactivity of porphyrins and related compounds. Part VI. Oxidative cleavage of the haem system. The four isomeric biliverdins of the IX seriesJournal of the Chemical Society, Perkin Transactions 1, 1973
- The electronic structure of the haem iron in haemoglobin Zurich β63his → argJournal of Molecular Biology, 1972
- Structural investigations of modified haemoglobins by nuclear magnetic resonance spectroscopyJournal of Molecular Biology, 1972
- HAEM catabolism and coupled oxidation of haemproteinsFEBS Letters, 1969
- The enzymatic conversion of heme to bilirubin by microsomal heme oxygenase.Proceedings of the National Academy of Sciences, 1968
- Molecular Pathology of Human HaemoglobinNature, 1968