Purified bile salt hydrolase from bile-adapted Xanthomonas maltophilia displays Michaelis-Menten kinetics on cholylglycine and cholyltaurine and hydrolyzes bile salts also in crude bovine bile. The protein is a dimer and is resistant to proteinases and to heating at 55 to 60°C for up to 60 min, in agreement with calorimetric data.

Characterization of Cholylglycine Hydrolase from a Bile-adapted Strain of Xantomonas maltophilia and its Application for Quantitative Hydrolysis of Conjugated Bile Salts

POLVERINO DE LAURETO, PATRIZIA;
2002

Abstract

Purified bile salt hydrolase from bile-adapted Xanthomonas maltophilia displays Michaelis-Menten kinetics on cholylglycine and cholyltaurine and hydrolyzes bile salts also in crude bovine bile. The protein is a dimer and is resistant to proteinases and to heating at 55 to 60°C for up to 60 min, in agreement with calorimetric data.
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11577/1361282
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