Tariq A.L and Reyaz A.L
The extracellular UTI associated protease produced from Serratia marcescens TW1. The protease was purified to homogeneity from the production medium by ammonium sulphateation, acetone precipitation with 80% saturation and DEAE cellulose column chromatography. The molecular weight of protease was found approximately 50 KDa weight by the sodium dodecyl sulfate polyacrylamide gel electrophoresis. The isoelectric point was close to 6.5. The maximal activity towards case in was found at 400C and its pH activity was maximum at 8.0. The protease was strongly inactivated by HgCl2 metal ion and reactivated by FeSO4 thus indicated as metalloprotease. The protease was inhibited by Na2EDTA. The antibodies rose against protease of Serratia marcescens strain TW1 when tested immunologically by showing line of precipitation against the antiserum thus indicated that protease is immunologically identical.
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