Lee W J, Adachi Y, Maki M, Hatanaka M, Murachi T
Department of Clinical Science, Kyoto University, Japan.
Biochem Int. 1990 Oct;22(1):163-71.
The mechanism for binding of human erythrocyte calpain I to human erythrocyte inside-out vesicles was studied by immunoelectrophoretic blot analysis. Binding of calpain I to inside-out vesicles was observed both in the absence and presence of Ca2+. Moreover, in the absence of Ca2+, acidic proteins like casein, ovalbumin and calpastatin suppressed while basic proteins like arginase and lysozyme did not affect the binding of calpain I to inside-out vesicles. Here, we propose a model for the binding of calpain to the membrane.
通过免疫电泳印迹分析研究了人红细胞钙蛋白酶I与人红细胞内翻囊泡的结合机制。在有无Ca2+的情况下均观察到钙蛋白酶I与内翻囊泡的结合。此外，在无Ca2+时，酪蛋白、卵清蛋白和钙蛋白酶抑制蛋白等酸性蛋白会抑制钙蛋白酶I与内翻囊泡的结合，而精氨酸酶和溶菌酶等碱性蛋白则不影响其结合。在此，我们提出了一个钙蛋白酶与膜结合的模型。
