Abstract
Cat haemoglobin binds 2 mol of triethyltin/mol of haemoglobin. Pretreatment of the haemoglobin with diethyl pyrocarbonate at pH6.0 prevents binding to one site only, whereas photo-oxidation with Methylene Blue removes both sites. Pretreatment of rat haemoglobin with diethyl pyrocarbonate also leads to the loss of one binding site. The possibility is discussed that the two binding sites for triethyltin on both cat and rat haemoglobin have a different chemical nature.
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Selected References
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- ALDRIDGE W. N., CREMER J. E. The biochemistry of organo-tin compounds; diethyltin dichloride and triethyltin sulphate. Biochem J. 1955 Nov;61(3):406–418. doi: 10.1042/bj0610406. [DOI] [PMC free article] [PubMed] [Google Scholar]
- ALLISON A. C., CECIL R. The thiol groups of normal adult human haemoglobin. Biochem J. 1958 May;69(1):27–34. doi: 10.1042/bj0690027. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Aldridge W. N., Street B. W. Oxidative phosphorylation. The specific binding of trimethyltin and triethyltin to rat liver mitochondria. Biochem J. 1970 Jun;118(1):171–179. doi: 10.1042/bj1180171. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Berger S. L. Diethyl pyrocarbonate: an examination of its properties in buffered solutions with a new assay technique. Anal Biochem. 1975 Aug;67(2):428–437. doi: 10.1016/0003-2697(75)90315-2. [DOI] [PubMed] [Google Scholar]
- Burstein Y., Walsh K. A., Neurath H. Evidence of an essential histidine residue in thermolysin. Biochemistry. 1974 Jan 1;13(1):205–210. doi: 10.1021/bi00698a030. [DOI] [PubMed] [Google Scholar]
- Holbrook J. J., Ingram V. A. Ionic properties of an essential histidine residue in pig heart lactate dehydrogenase. Biochem J. 1973 Apr;131(4):729–738. doi: 10.1042/bj1310729. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Lock E. A., Aldridge W. N. The binding of triethyltin to rat brain myelin. J Neurochem. 1975 Dec;25(6):871–876. doi: 10.1111/j.1471-4159.1975.tb04420.x. [DOI] [PubMed] [Google Scholar]
- Rose M. S., Aldridge W. N. Oxidative phosphorylation. The effect of anions on the inhibition by triethyltin of various mitochondrial functions, and the relationship between this inhibition and binding of triethyltin. Biochem J. 1972 Mar;127(1):51–59. doi: 10.1042/bj1270051. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rose M. S., Aldridge W. N. The interaction of triethyltin with components of animal tissues. Biochem J. 1968 Feb;106(4):821–828. doi: 10.1042/bj1060821. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rose M. S. Evidence for histidine in the triethyltin-binding site of rat haemoglobin. Biochem J. 1969 Jan;111(2):129–137. doi: 10.1042/bj1110129. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rose M. S., Lock E. A. The interaction of triethyltin with a component of guinea-pig liver supernatant. Evidence for histidine in the binding sites. Biochem J. 1970 Nov;120(1):151–157. doi: 10.1042/bj1200151. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Selwyn M. J., Dawson A. P., Stockdale M., Gains N. Chloride-hydroxide exchange across mitochondrial, erythrocyte and artificial lipid membranes mediated by trialkyl- and triphenyltin compounds. Eur J Biochem. 1970 May 1;14(1):120–126. doi: 10.1111/j.1432-1033.1970.tb00268.x. [DOI] [PubMed] [Google Scholar]
- York J. L., Roberts M. P. The iron and subunit binding sites of hemerythrin. The role of histidine, tyrosine and tryptophan. Biochim Biophys Acta. 1976 Feb 20;420(2):265–278. doi: 10.1016/0005-2795(76)90318-4. [DOI] [PubMed] [Google Scholar]
- van Assendelft O. W., Zijlstra W. G. Extinction coefficients for use in equations for the spectrophotometric analysis of haemoglobin mixtures. Anal Biochem. 1975 Nov;69(1):43–48. doi: 10.1016/0003-2697(75)90563-1. [DOI] [PubMed] [Google Scholar]
