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.

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