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PURIFICATION AND PROPERTIES OF AN ADENOSINETRIPHOSPHATASE

HEINZ RUPERT SCHREINER, University of Nebraska - Lincoln

Abstract

This thesis represents an attempt to elucidate the mode of action and the behavior of a heat stable enzyme, adenosine triphosphate-monophosphatase, from a thermophilic microorganism.The investigation of this enzyme was carried out in five distinct phases:One: A study of the distribution of adenosine tri- phosphate-monophosphatase activity in B. stearothermophilus, Isolate 2184.Two: The development of techniques suitable for the isolation of this enzyme and its purification to a degree considerably higher than reported before.Three: A kinetic and thermodynamic treatment of the inactivation of this enzyme by heat and a study of the influence of external conditions thereupon.Four: A kinetic and thermodynamic treatment of the activation of the enzymatically catalyzed reaction and a study of the formation of an intermediate enzyme-substrate complex.Five: The characterization of the highly purified adenosine triphosphate-monophosphatase.

Subject Area

Biochemistry

Recommended Citation

SCHREINER, HEINZ RUPERT, "PURIFICATION AND PROPERTIES OF AN ADENOSINETRIPHOSPHATASE" (1956). ETD collection for University of Nebraska-Lincoln. AAI0017365.
https://digitalcommons.unl.edu/dissertations/AAI0017365

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