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  • Title: Heterologous expression, purification, and properties of a potato protein inhibitor of serine proteinases.
    Author: Speranskaya AS, Krinitsina AA, Revina TA, Gerasimova NG, Keruchen'ko YS, Shevelev AB, Valueva TA.
    Journal: Biochemistry (Mosc); 2006 Nov; 71(11):1176-82. PubMed ID: 17140378.
    Abstract:
    The gene PKPI-B10 [AF536175] encoding in potato (Solanum tuberosum L., cv. Istrinskii) a Kunitz-type protein inhibitor of proteinases (PKPI) has been cloned into the pET23a vector and then expressed in Escherichia coli. The recombinant protein PKPI-B10 obtained as inclusion bodies was denatured, separated from admixtures by ion-exchange fast protein liquid chromatography (FPLC) on MonoQ under denaturing conditions, and renatured. The native protein was additionally purified by ion-exchange FPLC on DEAE-Toyopearl. The PKPI-B10 protein effectively inhibits the activity of trypsin, significantly weaker suppresses the activity of chymotrypsin, and has no effect on other serine proteinases: human leukocyte elastase, subtilisin Carlsberg, and proteinase K, and also the plant cysteine proteinase papain.
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