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. 2010 Dec 6;12(4):373–380. doi: 10.1111/j.1364-3703.2010.00679.x

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© 2010 THE AUTHORS. MOLECULAR PLANT PATHOLOGY © 2010 BSPP AND BLACKWELL PUBLISHING LTD

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In vitro proteolytic activity assays of purified Rsa1, renin, cathepsin D and Rsa1 mutant proteins. Each enzyme was treated with no inhibitor (□), 2 mm pepstatin A ( ) in 50 mm sodium phosphate buffer (pH 6.5) at 25 °C for 20 min, or 2 mm diazoacetyl‐d,l‐norleucine methyl ester (DAN) ( ) in 50 mm sodium phosphate buffer (pH 6.5) containing 0.13 mm CuSO₄ at 25 °C for 1 h. Values represent the means of triplicate samples. Vertical bars indicate standard deviations.

Inline graphic — In vitro proteolytic activity assays of purified Rsa1, renin, cathepsin D and Rsa1 mutant proteins. Each enzyme was treated with no inhibitor (□), 2 mm pepstatin A ( ) in 50 mm sodium phosphate buffer (pH 6.5) at 25 °C for 20 min, or 2 mm diazoacetyl‐d,l‐norleucine methyl ester (DAN) ( ) in 50 mm sodium phosphate buffer (pH 6.5) containing 0.13 mm CuSO₄ at 25 °C for 1 h. Values represent the means of triplicate samples. Vertical bars indicate standard deviations.