Dinitrophenol-Stimulated Adenosine Triphosphatase Activity in Extracts of Desulfovibrio gigas1
AUTOR(ES)
Guarraia, Leonard J.
RESUMO
A dinitrophenol (DNP)-stimulated adenosine triphosphatase (ATPase) has been found in both the soluble and particulate fractions of the anaerobic sulfate-reducing bacterium, Desulfovibrio gigas. As the soluble ATPase was labile to storage, only the particulate enzyme was studied in detail. It was optimally stimulated by DNP at 4 mm, and activity was insensitive to inhibition by ouabain. The ATPase was stimulated by both Ca2+ and Mg2+, but the magnitude of the stimulation was dependent upon pH. In the presence of Ca2+ the optimum pH was 6.5, whereas, in the presence of Mg2+ the pH optimum was 8.0. However, under optimal conditions the activity was the same with either Mg2+ or Ca2+. Both adenosine triphosphate and guanosine triphosphate were hydrolyzed, but activity toward guanosine triphosphate was only one-tenth that observed with adenosine triphosphate.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=248717Documentos Relacionados
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