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Digitale Medien

Partial purification and characterization of extracellular metalloproteases from Aeromonas salmonicida ssp. salmonicida (1995)

ARNESEN, J. A. ; EGGSET, G ; JØRGEN SEN, T. Ø.

Oxford, UK : Blackwell Publishing Ltd

Journal of fish diseases 18 (1995), S. 0

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ISSN: 1365-2761

Quelle: Blackwell Publishing Journal Backfiles 1879-2005

Thema: Biologie , Medizin

Notizen: Abstract. Aeromonas salmonicida ssp, salmonicida is shown to produce several extracellular proteins having gelatinolytic activity. Among the six isolates tested, two (NCMB 1102 and 84–14–R) produced both high (89–100 kDa) and low molecular (37 kDa) weight gelatinases, while the other four demonstrated only the 89–100 kDa forms. The low molecular form (metalloprotease 1: MP 1, 37 kDa) was isolated by ammonium sulphate precipitation, hydrophobic, ion exchange and size exclusion chromatography. The isolated enzyme was inhibited by the metal-chelating agents o-phenantroline and EDTA, and by excess Zn ions, and thus was defined as a metalloprotease. Its pH-optimum was 7–5, optimal activity was at 40°C and its pI 5.2. Specificity studies demonstrated cleavage of gelatin and azocoll, but not casein.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1111/j.1365-2761.1995.tb00305.x

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