Purification and Properties of Mutant and Wild-Type Diaphorases from Diplococcus pneumoniae

Optochin-resistant mutant and wild-type diaphorases were purified approximately 300-fold by a combination of batch adsorption and column chromatography with diethylaminoethyl cellulose, and were characterized with regard to their pH optima, sensitivity to optochin inhibition and heat inactivation, M...

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Dettagli Bibliografici

Pubblicato in:	J Bacteriol
Autori principali:	Kreger, Arnold S., Olsen, Ronald H.
Natura:	Artigo
Lingua:	Inglês
Pubblicazione:	American Society for Microbiology (ASM) 1968
Soggetti:	Microbial Physiology and Metabolism
Accesso online:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC252414/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/4386790/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.96.4.1029-1036.1968
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