Jan 20, 1976

Studies on the binding of haemoglobin by haptoglobin using electrofocusing and gradient electrophoresis

Biochimica Et Biophysica Acta
A V EmesF A Mulligan


1. Gel electrofocusing followed by gel gradient electrophoresis separated the haptoglobins and their complexes with haemoglobin into characteristic two-dimensional patterns of protein bands. 2. Molecular weights of 107 000, 139 000 and 168 000 were obtained for the three bands seen after a purified preparation of haptoglobin type 1 was partially saturated with haemoglobin. This indicated that free haptoglobin, the intermediate haptoglobin-haemoglobin complex containing one half-haemoglobin and the saturated complex with two half-haemoglobins were present. 3. The three proteins showed considerable microheterogeneity and gave a number of isoelectric points in the pH ranges 4.58-4.77, 5.20-5.40 and 5.74-5.93, free haptoglobin type 1 being the lowest group. These ranges were all 0.15-0.30pH units lower if other values were taken for the isoelectric points of markers used to calibrate the pH gradient. 4. All three proteins were present over a wide range of haemoglobin concentrations, from 0.5% to 92% of that required for saturation. This would be expected if both binding sites have similar affinities for haemoglobin.

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  • References2
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Mentioned in this Paper

Macromolecular Compounds
Plasma Protein Binding Capacity
Isoelectric Focusing
Hydrogen-Ion Concentration

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