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. 2014 Feb 21;19(2):2374–2389. doi: 10.3390/molecules19022374

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© 2014 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).

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Protein purification and proteolytic activity of AcCP2 expressed in yeast. (A) Immuno-detection of recombinant His-AcCP2 protein. Lane 1: AcCP2 crude proteins extracted from yeast containing the pPIC9K-His-AcCP2 vector; Lane 2: crude proteins extracted from yeast containing the pPIC9K empty vector; Lane 3: protein purification by Ni-NTA beads from yeast containing the pPIC9K-His-AcCP2 vector; Lane 4: the purified protein incubated at pH 4.3; and (B) Activity was measured on 1% Bz-Phe-Val-Arg-NH-Mec solution containing 15 mM AcCP2 proteinase under different pH. Data points represent the mean values of three replicates ± SE (n = 3).