Mechanical instability of the oxy-form of sickle haemoglobin.

摘要: MUCH attention has been given to the molecular aspects of deoxy form sickle haemoglobin (Hb S) because sickling occurs with Hb S in deoxygenated state. The oxy S, on other hand, is believed be similar normal adult A) respect solubility1,2, X-ray diffraction pattern3, oxygen binding4 and properties. During determination equilibrium curves we noticed that a solution oxyhaemoglobin became turbid very easily when it was stirred or mixed. turbidity found due protein which denatured by mechanical force involved and/or foaming. Oxyhaemoglobin more quickly than A mixing, stirring sonication. rate denaturation dependent concentration medium, suggesting an oxidative process involved. As demonstration requires only few drops blood, water shaking, this property can used as simple clinical test for presence S.