Characterization, purification, and DNA sequence analysis of a novel ATPase of the archaebacterium Methanococcus voltae

Membrane-bound ATPase activity was detected in the methanogen Methanococcus voltae. The ATPase was inhibited by vanadate, a characteristic inhibitor of the P type ATPases. The enzyme activity was also inhibited by diethylstilbestrol. However, it was insensitive to N,N$\sp\prime$-dicyclohexylcarbodiimide, bafilomycin A$\sb1$, nitrate, ouabain and oligomycin. The enzyme displayed a high preference for ATP as substrate, was dependent on Mg$\sp{2+}$, and had a pH optimum of 7.5. The enzyme was completely solubilized with 2% Triton X-100. It was insensitive to oxygen and was stabilized by ATP.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Biology

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2011

Author dc:creator

• Dharmavaram, Rita M.

Contributors dc:contributor

• Konisky, Jordan

• Biology, Cell

Statement dc:rights

• Copyright 1990 Dharmavaram, Rita M.

Language dc:language

eng

Identifier

AAI9114220
(UMI)AAI9114220

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/22342