The effect of pH on the rate of dissociation of the oxygenated beta chain tetramer of Hb A
Biochemical and Biophysical Research Communications, ISSN: 0006-291X, Vol: 111, Issue: 1, Page: 55-60
1983
- 4Citations
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Metrics Details
- Citations4
- Citation Indexes4
- CrossRef4
Article Description
The effect of pH on the overall assembly of oxyhemoglobin A following mixing of equivalent concentrations of α and β heme subunits has been studied in 0.1 M potassium phosphate buffers at 20°C. The resultant kinetic profiles monitored at 582.5 nm (the maximum of the oxyhemoglobin — oxy chain difference spectrum) were homogeneous and appeared to be first order. The rate of these exponential time courses, reflecting the rate of dissociation of the β chain tetramer, increased from 0.013 min −1 at pH 6.4 to 0.30 min −1 at pH 8.0 and 1.0 min −1 at pH 8.5. Concurrent with this increased rate was a decrease in the overall color yield from the reaction. The absorbance changes, which involve a significant contribution from the β chain tetramer to monomer dissociation step, changed three fold over the pH range studied. The findings indicate that protons enhance the stability of the β chain tetramer.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0006291X83801168; http://dx.doi.org/10.1016/s0006-291x(83)80116-8; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0020538228&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/6830601; http://linkinghub.elsevier.com/retrieve/pii/S0006291X83801168; http://api.elsevier.com/content/article/PII:S0006291X83801168?httpAccept=text/xml; http://api.elsevier.com/content/article/PII:S0006291X83801168?httpAccept=text/plain; https://linkinghub.elsevier.com/retrieve/pii/S0006291X83801168; http://dx.doi.org/10.1016/s0006-291x%2883%2980116-8; https://dx.doi.org/10.1016/s0006-291x%2883%2980116-8
Elsevier BV
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