[Purification and characteristics of creatininase from Arthrobacter sp].
A creatininase produced from a Arthrobacter sp. was purified 145-fold by a series of steps including heat treatment, ammonium sulfate precipitation, DEAE-Cellulose ion-exchange and hydrophobic chromatography. The specific activity of the pure enzyme was 209u/mg. The subunit molecular mass of creatininase was estimated to be 33 700D by SDS-PAGE. The creatininase was stable in the pH range between 6.0 - 9.0 and below 60 degrees C . Its Km value for creatinine was estimated to be 21.14 mmol/L. The enzyme was markedly inactivated by incubation with 1 mmol/L of Hg2+, Ag2+, Li+, Cu2+ and 20 mmol/L of 1, 11-Phananthroline respectively. Activation was observed when the enzyme was incubated with 1 mmol/L of Co2+ and Mn2+.
Zhao
Geng-Feng
GF
College of Life Sciences, Zhejiang University, Hangzhou 310029, China.
Ma
Xiao-Hang
XH
Jia
Xiao-Ming
XM
Zhao
Yu-Hua
YH
Wang
Yuan-Yuan
YY
D000581:Amidohydrolases / Q000302:isolation & purification* / Q000378:metabolism*; D001173:Arthrobacter / Q000201:enzymology*; D001426:Bacterial Proteins / Q000302:isolation & purification* / Q000378:metabolism; D002848:Chromatography, DEAE-Cellulose / Q000379:methods
D001426:Bacterial Proteins; D000581:Amidohydrolases; C019946:creatininase