TY - JOUR
T1 - Resolution of the Hemolytic and the Hydrolytic Activities of Phospholipase‐C Preparation from Clostridium perfringens
AU - Sabban, Esther
AU - Laster, Yehudith
AU - Loyter, Abraham
PY - 1972/7
Y1 - 1972/7
N2 - Phospholipase‐C preparations from Clostridium perfringens can induce hemolysis of chicken erythrocytes in the presence of EDTA. Under these conditions hydrolysis of membrane phospholipids does not take place. When Ca2+ is added to the incubation media both hemolysis and hydrolysis of phospholipids occur. However, when Mn2+ or UO22+ is added, both the hemolysis and hydrolysis of membrane phospholipids are strongly inhibited. When phospholipase‐C (Cl. perfringens) preparations are heated at 56°C in the presence of Ca2+, the hemolytic activity is inhibited while the hydrolytic activity of the enzyme is retained. Such non‐hemolytic phospholipase‐C barely hydrolyse phospholipids from intact chicken red‐blood cells. However, it readily hydrolyses phospholipids from erythrocyte ghosts. Thus it appears that membrane phospholipids are unavailable to the enzyme unless they are exposed by hemolysis.
AB - Phospholipase‐C preparations from Clostridium perfringens can induce hemolysis of chicken erythrocytes in the presence of EDTA. Under these conditions hydrolysis of membrane phospholipids does not take place. When Ca2+ is added to the incubation media both hemolysis and hydrolysis of phospholipids occur. However, when Mn2+ or UO22+ is added, both the hemolysis and hydrolysis of membrane phospholipids are strongly inhibited. When phospholipase‐C (Cl. perfringens) preparations are heated at 56°C in the presence of Ca2+, the hemolytic activity is inhibited while the hydrolytic activity of the enzyme is retained. Such non‐hemolytic phospholipase‐C barely hydrolyse phospholipids from intact chicken red‐blood cells. However, it readily hydrolyses phospholipids from erythrocyte ghosts. Thus it appears that membrane phospholipids are unavailable to the enzyme unless they are exposed by hemolysis.
UR - http://www.scopus.com/inward/record.url?scp=0015522006&partnerID=8YFLogxK
U2 - 10.1111/j.1432-1033.1972.tb01923.x
DO - 10.1111/j.1432-1033.1972.tb01923.x
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C2 - 4342909
AN - SCOPUS:0015522006
SN - 0014-2956
VL - 28
SP - 373
EP - 380
JO - European Journal of Biochemistry
JF - European Journal of Biochemistry
IS - 3
ER -