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• W1909696021 abstract "A proteinase of Mr 27,000 with a possible role in the metabolism and invasion of host tissues was purified from the conditioned medium of Trichophyton rubrum by concanavalin A and anion-exchange chromatography. Peaks of proteolytic activity were analyzed by substrate gel electrophoresis. The 27,000-Mr proteinase had a pH optimum of 8.0, a calcium dependence of 2 mM, and was inhibited by serine proteinase inhibitors, especially phenylmethylsulfonyl fluoride and Phe-Gly-Ala-Leu-chloromethyl ketone. By polyacrylamide gel electrophoresis, the 27,000-Mr proteinase had a reduced molecular weight of 44,000 and reacted with [3H]diisopropyl fluorophosphate. The proteinase degraded azocoll, type III collagen, type IV procollagen, laminin, fibronectin, and the peptide substrates succinyl-Ala-Ala-Pro-Phe-p-nitroanilide (1,573 M-1 s-1) and t-butyloxy carbonyl-Ala-Ala-Leu-p-nitroanilide (1,614 M-1 s-1)." @default.
• W1909696021 created "2016-06-24" @default.
• W1909696021 creator A5047604786 @default.
• W1909696021 creator A5050856602 @default.
• W1909696021 date "1989-10-01" @default.
• W1909696021 modified "2023-09-26" @default.
• W1909696021 title "Purification and characterization of a 27,000-Mr extracellular proteinase from Trichophyton rubrum" @default.
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• W1909696021 doi "https://doi.org/10.1128/iai.57.10.3072-3080.1989" @default.
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