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艾氏腹水瘤细胞和猪肾中钙激活中性硫醇蛋白酶对所有中间丝亚基蛋白的高效体外降解作用。

Efficient degradation in vitro of all intermediate filament subunit proteins by the Ca2+-activated neutral thiol proteinase from Ehrlich ascites tumor cells and porcine kidney.

作者信息

Vorgias C E, Traub P

出版信息

Biosci Rep. 1986 Jan;6(1):57-64. doi: 10.1007/BF01145179.

Abstract

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.

摘要

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。

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