Collect. Czech. Chem. Commun. 1981, 46, 1288-1295

The conformational changes of haemoglobin on its binding to haptoglobin

Barbora Dvořánková and Zdeněk Pavlíček

Department of Physical Chemistry, Charles University, 128 40 Prague 2


The binding of human haemoglobin to human haptoglobin has been found to alter the conformation of haemoglobin. Spectrophotometric measurements, measuring of peroxidase activity, thin-layer gel chromatography and modelling on an analogue computer led to the conclusion that the binding of haemoglobin to haptoglobin was associated with a change in the quaternary structure of haemoglobin, with a transition from the R state to the T state. The kinetics of the conformational changes had an autocatalytic character.