Collect. Czech. Chem. Commun. 1981, 46, 1990-1993

Changes in human haemoglobin after its reaction with glutaraldehyde

Václava Fričová, Tomáš I. Přistoupil, Marie Kramlová, Stanislav Ulrych and Tomáš Mařík

Institute of Haematology and Blood Transfusion, 128 20 Prague 2


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.