Abstract
Trichophyton mentagrophytes is able to produce extracellular keratinolytic proteases with an apparently pronounced substrate specificity. The molecular weights of the two observed enzymes are 80 and 200 kilodaltons as determined by SDS pore gradient gel electrophoresis. The isoelectric point of the main enzyme is 6.7; the optimum pH for lysis of guinea pig hair is 7.5. Bifonazole exerts an effect on the in vitro secretion of the protein at the nanogram level, which is far lower than its in vitro MIC level (20 ng/ml as against 0.25–2 µg/ml MIC). Even at 0.6–0.8 ng/ml bifonazole the in vitro lytic activity was reduced to 50% compared with untreated controls.
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References
Negi M, Tsuboi R, Matsui T, Ogawa H (1984) Isolation and characterisation of proteinase from Candida albicans: substrate specificity. J Invest Dermatol 83 (1): 32–36
Takiuchi I, Higuchi D, Yoshihiro S, Koga M (1982) Isolation of an extracellular proteinase (keratinase) from Microsporum canis. Sabouraudia 20: 281–288
Yu RJ, Harmon SR, Wachter PE, Blank F (1969) Amino acid composition and specificity of a keratinase of Trichophyton mentagrophytes. Arch Biochem Biophys 135: 363–370
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© 1986 Springer-Verlag Berlin Heidelberg
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Abbink, J., Plempel, M., Berg, D. (1986). Expression of Keratinolytic Activity by Trichophyton mentagrophytes . In: Hay, R.J. (eds) Advances in Topical Antifungal Therapy. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-71717-8_3
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DOI: https://doi.org/10.1007/978-3-642-71717-8_3
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-540-17302-1
Online ISBN: 978-3-642-71717-8
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