Novel trypsin inhibitors from the white rot fungus Abortiporus biennis. Partial purification and characterization |
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Authors: | J. Zuchowski M. Jaszek K. Grzywnowicz |
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Affiliation: | (1) Department of Biochemistry and Crop Quality, Institute of Soil Science and Plant Cultivation, ul. Czartoryskich 8, 24-100 Pulawy, Poland;(2) Department of Biochemistry, M. Curie-Sklodowska University, pl. M. Curie-Sklodowskiej 3, 20-031 Lublin, Poland |
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Abstract: | Novel trypsin inhibitors from the white rot fungus Abortiporus biennis were isolated, partially purified, and char- acterized. The inhibitors were purified by heat treatment, anion-exchange chromatography, and gel filtration. SDS-PAGE of the purified preparation demonstrated the presence of two proteins with molecular masses of 20 and 21.5 kDa. The A. biennis inhibitors were most active against trypsin, while chymotrypsin α, proteinase K, and Carlsberg subtilisin were inhibited to a smaller extent. The inhibitors are acidic proteins with remarkably high heat stability. Published in Russian in Biokhimiya, 2009, Vol. 74, No. 2, pp. 278–283. |
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Keywords: | Abortiporus biennis protease inhibitors white rot fungi Basidiomycetes |
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