Purification and some characteristics of phosphatase of a psychrophile

Journal of Biochemistry
H TsurutaYasuo Aizono

Abstract

The phosphatase of a psychrophile was purified by ammonium sulfate fractionation, and a sequence of chromatographies on DEAE-Cellulofine, butyl-Cellulofine, Sephacryl S-100, and Mono-Q columns. The purified enzyme preparation was found to be electrophoretically homogeneous on native- and SDS-PAGE, and its molecular mass was determined to be 38.4 kDa by MALDI-TOF mass spectrometry. Maximal activity was observed at 30 degrees C and pH 6.0. Furthermore, the activity of this enzyme at 0 and 5 degrees C was 27 and 28%, respectively, of that at 30 degrees C. The enzyme was stable in the pH range of 6.0 to 8.0 and up to 20 degrees C. The enzyme was affected by metal ions; the activity was enhanced by Mg2+ and Ca2+ ions, but depressed by Zn2+ ions. Analysis of the amino acid composition indicated that this phosphatase contains no S-S bond, and only a few prolyl residues necessary to retain the rigid structure of a protein molecule. The phosphatase shows typical features of a cold enzyme; high catalytic activity at low temperature and rapid inactivation at an intermediate temperature.

Citations

Nov 7, 2002·Biochemical and Biophysical Research Communications·Yuko YamanakaKenji Soda
Jan 11, 2001·Biochimica Et Biophysica Acta·P P SheridanJ E Brenchley
Aug 28, 2003·Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology·Bjarni AsgeirssonPeter Højrup
Feb 15, 2000·European Journal of Biochemistry·M RinaV Bouriotis
Oct 12, 2007·Bioscience, Biotechnology, and Biochemistry·Hiroki TsurutaYasuo Aizono
Feb 24, 2005·Bioscience, Biotechnology, and Biochemistry·Yutaka SuzukiShigenori Kanaya
Jan 1, 1998·Bioscience, Biotechnology, and Biochemistry·Y IshidaY Aizono

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