Summary
Rubescenslysin from the edible mushroom Amanita rubescens (Pers. ex Fr.) Gray is an acidic protein that directly lyzes red cells. It is active even in the absence of Ca2+ and Mg2+ and its activity is not influenced by cysteine. — The concentration-response curve is steep. The time-course of haemolysis is characterized by a rather long lag phase; but after the onset of the haemolysis it proceeds quickly. The rate of haemolysis increases and the lag phase decreases with increasing lysin concentrations. The pH optimum is in the weekly acid range and the optimal temperature is 35°C. A pronounced increase in the neutral salt concentration inhibits the haemolysis; a self-inhibition is observed at higher lysin concentrations, particularly with preparations with a small degree of purity. — The haemolysis is of the osmotic type: a marked prelytic leakage of potassium as observed as well as a significant decrease of osmotic resistance on treatment of red cells with sublytic lysin concentrations. — Red cell sensitivity of various animal species decreases in the order: rat ≃ guinea pig = man = mouse ≃ dog ≃ rabbit > pig > cat > cattle = sheep; on the whole, species specifity is small. — The rubescenslysin haemolysis is inhibited by heavy metal salt (Cu2+>Fe2+>Zn2+>Cd2+>Mn2+>Ni2+) and by pretreatment of the erythrocytes with glutardialdehyde and wheat germ lectin > soya bean lectin. — Rubescenslysin is consumed on haemolysis and markedly inhibited by haemolysate (from bovine blood) as well as by red cell ghosts (from bovine and sheep blood). It is also inhibited by cholesterol and various phospholipids: sphingomyelin from bovine brain > sphingomyelin from chicken egg > phosphatidyl choline from egg yolk > phosphatidyl ethanolamine from dog brain; no inhibition is produced by phosphatidyl ethanolamine from bovine brain or soya bean. Of the synthetic phosphatidyl cholines dimyristoyl- has a stronger inhibitory effect than dipalmitoyl- and distearoyl-; on the other hand, dilauroyl- or dioleoyl- has no inhibitory effect. Human serum albumin or pretreatment of the erythrocytes with trypsin does not affect the haemolytic activity of rubescenslysin. — Surface activity of a rubescenslysin solution is greater than that of a serum albumin solution of the same concentration. — The results allow the conclusion that the cytolytic effect of rubescenslysin is due to a detergent activity of this protein.
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Seeger, R. Studies on rubescenslysin haemolysis. Naunyn-Schmiedeberg's Arch. Pharmacol. 311, 95–103 (1980). https://doi.org/10.1007/BF00500309
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DOI: https://doi.org/10.1007/BF00500309