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PMID: 824266 Published · ppublish English Journal Article

Localization of tetramethylphenylenediamine-oxidase in the outer cell wall layer of Neisseria meningitidis.

Journal of bacteriology ·Vol. 128 ·No. 1 ·1976-10-00 ·Pages 144-8

Devoe IW, Golchrist JE

Abstract

A highly active tetramethylphenylenediamine-oxidase has been found in association with the cell wall blebs, evaginations of the outer wall membrane, of Neisseria meningitidis. Isolated wall blebs consumed oxygen in the presence of ascorbate-tetramethylphenylenediamine but not in the presence of succinate, whereas cell envelope preparations are active in both substrates. The ratio of succinate dehydrogenase/tetramethylphenylenediamine-oxidase activities in preparations of envelopes was approximately 100 times that in isolated wall blebs, indicating that the outer membrane preparations were highly purified.

MeSH Terms
Cell Fractionation Cell Wall/enzymology Cyanides/pharmacology Neisseria meningitidis/enzymology,metabolism,ultrastructure Oxidoreductases/isolation & purification,metabolism Oxygen Consumption Succinate Dehydrogenase/metabolism Tetramethylphenylenediamine
Chemicals
Cyanides Oxidoreductases Succinate Dehydrogenase Tetramethylphenylenediamine
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Devoe I W
Golchrist J E
References (10)
10 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1976-10-00
Pages
144-8
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC232836
Subset
IM
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