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• W2011714009 abstract "A serine proteinase from Penicillium citrinum was purified. The M(r) and isoelectric point were determined as about 26,000 and 9.5, respectively. Activity was retained up to above 40 degrees at pH 7 for 30 min, but the enzyme was completely inactivated at 50 degrees. The first amino acids in the N-terminal region were ANVVQSNVPSWGLARISSKRPGTTSYTYDSTAGEGVVFYGVDTG. The specificity differs from that of other serine proteinases. Kinetic studies on fluorogenic substrates were determined." @default.
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• W2011714009 date "1993-01-01" @default.
• W2011714009 modified "2023-10-18" @default.
• W2011714009 title "A heat-labile serine proteinase from Penicillium citrinum" @default.
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• W2011714009 doi "https://doi.org/10.1016/0031-9422(93)85144-g" @default.
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