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Biochemical Study of Inorganic Pyrophosphatase Isolated from Escherichia coli | ||
| Tikrit Journal of Pure Science | ||
| Article 1, Volume 14, Issue 2, 2009, Pages 308-313 | ||
| Abstract | ||
| The study concerned with describing the activity and some properties of the enzyme inorganic pyrophosphatase (EC 3.6.1.1) from Escherichia coli. A high activity of the enzyme was detected in Escherichia coli. The highest specific activity of the enzyme was detected in the supernatant (466) nmol/min/mg protein and the lowest was in the precipitant, by a sonication and centrifugation, (98) nmol/min/mg protein, while crude extract exhibited a value between the two limits (420) nmol/min/mg protein. The optimum conditions of the enzyme activity were (300) mg protein as a source of enzyme, (2.0) mmol of sodium pyrophosphate as a substrate, at pH (7.0) , with (10) minutes as incubation time at 37C and the Michaelis-Menten constant (Km) was about (0.42) mmol. | ||
| Keywords | ||
| Escherichia coli; inorganic pyrophosphatase | ||
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