| Literature DB >> 3913327 |
M Ameyama, M Nonobe, E Shinagawa, K Matsushita, O Adachi.
Abstract
An improved enzymatic method for the determination of pyrroloquinoline quinone, a novel prosthetic group of some important oxidoreductases, has been developed with cytoplasmic membrane of Escherichia coli K-12, in which D-glucose dehydrogenase (EC 1.1.99.17) was completely resolved to apo-enzyme by EDTA treatment. Incubation of the EDTA-treated membrane with exogenous pyrroloquinoline quinone in the presence of magnesium ions gave a quantitative determination of pyrroloquinoline quinone by assaying the restored D-glucose dehydrogenase activity. This novel enzymatic method was confirmed to be highly reproducible up to 10 ng of pyrroloquinoline quinone and could be applied to a routine assay of pyrroloquinoline quinone.Entities:
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Year: 1985 PMID: 3913327 DOI: 10.1016/0003-2697(85)90174-5
Source DB: PubMed Journal: Anal Biochem ISSN: 0003-2697 Impact factor: 3.365