Partial Characterization of a Trypsin-Stimulated Cytoplasmic Soluble Adenosine Triphosphatase of Agrobacterium Tumefaciens
1 Department of Microbiology University of Ife, Ile-Ife, Nigeria.
* Corresponding author: olusolaoshonukan@nsmjournal.org.ng
* Corresponding author: olusolaoshonukan@nsmjournal.org.ng
Abstract
A cold-labile trypsin-stimulated adenosine triphosphatase, ATPase (EC. 3.6.1.3) activity has been found associated with the partially purified cytoplasmic soluble fraction of Agrobacterium tumefaciens strain C-58. Chromatographic, electrophoretic, and catalytic studies are also reported. Trypsin activated the enzyme 31% at the pH optimum of between 8.0 and 9.0. The optimum temperature of activity for the enzyme was between 28°C and 50°C, whereas the enzyme was better maintained for several days at 4°C than either at 28°C or 37°C.
Keywords
cold-labile trypsin-stimulated adenosine triphosphatase
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How to Cite
Shonukan, O. O. (1982). Partial Characterization of a Trypsin-Stimulated Cytoplasmic Soluble Adenosine Triphosphatase of Agrobacterium Tumefaciens. Nigerian Journal of Microbiology, 2(2), 195-206. https://doi.org/10.67614/njm.1982.bdon2ms1
O. O. Shonukan, "Partial Characterization of a Trypsin-Stimulated Cytoplasmic Soluble Adenosine Triphosphatase of Agrobacterium Tumefaciens," Nigerian Journal of Microbiology, vol. 2, no. 2, pp. 195-206, December 1982. doi: 10.67614/njm.1982.bdon2ms1
