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首页> 外文期刊>Infection and immunity >Purification and characterization of a 27,000-Mr extracellular proteinase from Trichophyton rubrum.
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Purification and characterization of a 27,000-Mr extracellular proteinase from Trichophyton rubrum.

机译：红毛癣菌中一种27,000-Mr的胞外蛋白酶的纯化和鉴定。

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摘要

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).
机译：通过伴刀豆球蛋白A和阴离子交换色谱法从红毛癣菌的条件培养基中纯化了Mr 27,000的蛋白酶，该蛋白酶可能在宿主组织的代谢和侵袭中起作用。蛋白水解活性的峰通过底物凝胶电泳分析。 27,000-Mr蛋白酶的最适pH为8.0，钙依赖性为2 mM，并被丝氨酸蛋白酶抑制剂（尤其是苯甲基磺酰氟和Phe-Gly-Ala-Leu-氯甲基酮）抑制。通过聚丙烯酰胺凝胶电泳，该27,000-Mr蛋白酶具有降低的分子量44,000，并与[3H]二异丙基氟磷酸盐反应。蛋白酶降解的偶氮唑，III型胶原蛋白，IV型胶原蛋白，层粘连蛋白，纤连蛋白和肽底物琥珀酰-Ala-Ala-Pro-Phe-对硝基苯胺（1,573 M-1 s-1）和叔丁氧基羰基-Ala -Ala-Leu-对硝基苯胺（1614 M-1 s-1）。

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