Abstract
Structural investigations of the glycoprotein, Mucor miehei protease, by CD, suggested that the native enzyme contains a significant amount of β structure and little, if any, α-helix within the pH range 2.5 to 7.0. Comparison of the CD spectra of the protease with those of other proteins suggested somewhat distorted β arrangements. Exposure of the enzyme to periodate oxidation resulted in a rapid loss of about 40% of the carbohydrate but no detectable change in structure or enzymatic activity. The remainder of the carbohydrate was resistant to further oxidation; any additional decrease being associated with changes in structure and loss of proteolytic activity.
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