Vorgias C E, Traub P
Biosci Rep. 1986 Jan;6(1):57-64. doi: 10.1007/BF01145179.
Vimentin, desmin, glial fibrillary acidic protein, neurofilament triplet proteins, and a mixture of cytokeratins were digested with Ca2+-activated neutral thiol proteinase isolated from Ehrlich ascites tumor (EAT) cells and porcine kidney. All intermediate filament proteins were degraded by the proteinase, although with different rates and Ca2+ optima. These results are in part at variance with our previous statement that the Ca2+-activated proteinase from EAT cells is specific for vimentin and desmin.
波形蛋白、结蛋白、胶质纤维酸性蛋白、神经丝三联体蛋白以及细胞角蛋白混合物，用从艾氏腹水瘤（EAT）细胞和猪肾中分离出的Ca2+激活的中性巯基蛋白酶进行消化。尽管消化速率和Ca2+最佳浓度不同，但所有中间丝蛋白都被该蛋白酶降解。这些结果与我们之前关于EAT细胞中Ca2+激活的蛋白酶对波形蛋白和结蛋白具有特异性的说法部分不一致。
