Abstract
An improved method for the isolation of Mucor miehei protease which utilizes a diafiltration cell has been used to obtain a highly purified protein in gram quantities and yields of about 80%. Based on a modified molecular weight function and data from amino acid analysis, a value of 41 800 for the molecular weight of the glycoprotein was established and some modification to the published amino acid composition was made. These results suggest that Mucor miehei protease is distinctly different from the two other acid proteases which are also produced by species of Mucor.

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