[Interconnection between the structure and protective action of normal and pathological ceruloplasmin preparations in copper-induced erythrocyte lysis].

It was found that the differences in the protective effects of ceruloplasmin (CP) isolated from the blood of healthy donors and of the ceruloplasmin-like protein (pat-CP) isolated from the blood of patients with hepatovertebral dystrophy (HCD) during Ca(2+)-induced lysis of erythrocytes (RBC) result from significant changes in the carbohydrate fragment of pat-CP, the bulk of which (65%) is devoid of mannose and acetylglucosamine residues. According to the data from lentil-lectin Sepharose chromatography, only 4% of pat-CP molecules contain the [formula; see text] fragment necessary for the binding to ER receptors. The curves reflecting the Cu2+ accumulation in healthy donor ER and in pat-CP during the Cu(2+)-induced lysis were found to differ significantly. The ability of pat-CP to prevent the accumulation of Cu2+ in ER and pat-ER was markedly decreased compared with CP. Besides, CP prevented the diminution of reduced glutathione (GSH) in ER in a greater degree than pat-CP, whereas pat-ER, in contrast with CP, had no effect on the GSH concentration in pat-ER. It is suggested that the reactions occurring in the cell during Cu(2+)-induced lysis of ER and pat-ER are different.