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The heterogeneity and molecular weight of human haemoglobin derivatives after their reaction with glutaraldehyde was examined. When subjected to polyacrylamide gel electrophoresis the intact and modified haemoglobin markedly differ: the former shows two fractions in the molecular weight range of 20 000 daltons whereas a series of fractions of molecular weight of 35 000-100 000 daltons are observed after the reaction with glutaraldehyde. Simultaneously the dissociation curves of oxyhaemoglobin vary as a function of glutaraldehyde concentration. The samples of modified haemoglobin show a higher affinity for oxygen than intact haemoglobin.

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