Haemoglobulin catabolism: the role of ferrihaems in studies of the degradation pathway (Short Communication)
- 1 January 1974
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 137 (1) , 135-137
- https://doi.org/10.1042/bj1370135
Abstract
The importance of ferrihaem aggregation in studies of haemoglobin catabolism is assessed in the light of recent work. Experimental evidence is put forward suggesting that monomeric ferrihaems are degraded much more readily than dimeric species. This may offer an alternative explanation for the apparent ‘apoprotein catalysis’ recently observed.Keywords
This publication has 10 references indexed in Scilit:
- The catalase activity of ferrihaemsBiochemical Journal, 1973
- Oxidation of deuteroferrihaem by hydrogen peroxideBiochemical Journal, 1973
- Enzymic degradation of heme. Oxygenative cleavage requiring cytochrome P-450Biochemistry, 1972
- The degradation of haem by mammals and its excretion as conjugated bilirubin.1972
- Non-enzymic nature of the pyridine haemochrome-cleaving activity of mammalian tissue extracts (‘haem α-methyl oxygenase’)Biochemical Journal, 1970
- Catalatic activity of iron(III)-centred catalysts. Role of dimerization in the catalytic action of ferrihaemsBiochemical Journal, 1970
- Aggregation of ferrihaems. Dimerization and protolytic equilibria of protoferrihaem and deuteroferrihaem in aqueous solutionBiochemical Journal, 1970
- HAEM catabolism and coupled oxidation of haemproteinsFEBS Letters, 1969
- Solution structures of ferrihaem in some dipolar aprotic solvents and their binary aqueous mixturesBiochemical Journal, 1969
- Bile pigment formation in vitro from haematin and haem derivativesBiochemical Journal, 1954