TY - JOUR
T1 - Proteolytic self-digestion of bovine erythrocyte membranes
AU - Gaczyńska, Maria
AU - Bartosz, Grzegorz
AU - Rosin, Janusz
AU - Soszyński, Mirosław
PY - 1985
Y1 - 1985
N2 - 1. 1. "Self-digestion" of bovine erythrocyte membrane proteins was studied in isolated membrane preparations during prolonged incubation at 37 C. 2. 2. Protcase activities associated with the membrane result in progressive degradation of all main erythrocyle membrane proteins, in particular spectrin and Band 3. and formation of lower molecular weight products which have been tentatively assigned to parent molecules. 3. 3. Membrane protein "self-digestion" occurs in a broad pH range (2-11), is inhibited by increased ionic strength and by inhibitors of metalloproteases. cysteine and serine proteases. and activated by low concentrations of SDS. 4. 4. "Self-digestion" also takes place in NaOH-stripped erythrocyte membranes. 5. 5. The activity of a protease involved in the "self-digestion", of apparent molecular weight of about 35,000, was renatured after SDS-polyacrylamide gel electrophoresis of erythrocyte membrane proteins.
AB - 1. 1. "Self-digestion" of bovine erythrocyte membrane proteins was studied in isolated membrane preparations during prolonged incubation at 37 C. 2. 2. Protcase activities associated with the membrane result in progressive degradation of all main erythrocyle membrane proteins, in particular spectrin and Band 3. and formation of lower molecular weight products which have been tentatively assigned to parent molecules. 3. 3. Membrane protein "self-digestion" occurs in a broad pH range (2-11), is inhibited by increased ionic strength and by inhibitors of metalloproteases. cysteine and serine proteases. and activated by low concentrations of SDS. 4. 4. "Self-digestion" also takes place in NaOH-stripped erythrocyte membranes. 5. 5. The activity of a protease involved in the "self-digestion", of apparent molecular weight of about 35,000, was renatured after SDS-polyacrylamide gel electrophoresis of erythrocyte membrane proteins.
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U2 - 10.1016/0020-711X(85)90014-X
DO - 10.1016/0020-711X(85)90014-X
M3 - Article
C2 - 3908185
AN - SCOPUS:0022370844
VL - 17
SP - 1237
EP - 1245
JO - International Journal of Biochemistry
JF - International Journal of Biochemistry
SN - 1357-2725
IS - 11
ER -