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Abstract
Hemoglobin is a tetrameric protein which is able to dissociate into dimers. The dimers can in turn dissociate into tetramers. It has been found that dimers are more reactive than tetramers. The difference in the reactivity of these two species has been used to determine the tetramerdimer dissociation constant of various derivatives of rabbit hemoglobin. The constant has been found to be the same for all the derivatives of rabbit hemoglobin, implying that the ligand bound on the heme has no significant effect on the tetramer-dimer dissociation of rabbit hemoglobin. African Journal of Educational Studies in Mathematics and Sciences Vol. 5 2007: pp. 71-76
Highlights
Proteins are capable of undergoing aggregation-disaggregation and association-dissociation
By inputting the values of transmittance as a function of time into a computer programme written for this purpose
A is the initial concentration of dithiobis-(2nitrobenzoic acid) (DTNB) in M; b is the concentration of reacting sulphydryl groups in M; and x is the time dependent concentration of 2-thio-5-nitrobenzoate (TNB) in M
Summary
Proteins are capable of undergoing aggregation-disaggregation and association-dissociation. The former occurs in the form of protein-protein interactions involving high molecular weight proteins. An example is the aggregation of hemoglobin S molecules to form long fibres. The formation of the bond is an aggregation process. In cases of chronic renal failure, oxidized glutathione may react with hemoglobin, leading to protein aggregation in erythrocytes, which in turn leads to hemolysis. This is important in the pathogenesis of anemia in hemodialyzed patients 4
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