Pasteurization affects the physicochemical properties and biological function of hemoglobin? / 中国组织工程研究

ABSTRACT

BACKGROUND:Pasteurization is a perfect method for albumin virus inactivation, which may not be required for virus inactivation validation. However, there are no systematical reports concerning virus inactivation of hemoglobin blood substitutes. OBJECTIVE:To explore the effects of pasteurization on the physicochemical properties and biological function of hemoglobin blood substitutes. METHODS:Appropriate cord blood samples were taken fol owed by centrifugation, washing blood, rupture of membranes, stabilizer treatment. In the control group, the samples were placed in 55℃water bath, and when the temperature of hemoglobin solution reached (55±1)℃, a heat treatment began and lasted for 2 hours. In the pasteurization group, the samples were placed in 60℃water bath, and when the temperature of hemoglobin solution reached (60±1)℃, a heat treatment began and lasted for 10 hours. The heating process was under continues nitrogen protection. Then, the hemoglobin solution was placed in ice bath and cooled to below 4℃fol owed by low-speed centrifugation and filtration via microporous membrane, purification and viral inactivation thereby to obtain cord blood hemoglobin. RESULTS AND CONCLUSION:The products in the pasteurization group were al red clear liquid. There was no significant difference between the two groups in the yield, methemoglobin concentration, and oxygen-carrying capacity. The purification of the two groups was more than 98%. Two kinds of purification methods had no effects on the oxygen-carrying capacity of hemoglobin. Therefore, pasteurization method can replace thermosensitive purification method of 55℃, 2 hours. The pasteurization method wil not only ensure the physicochemical and biological properties of hemoglobin, but also achieve the purpose of virus inactivation.