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1. Electron-transferring flavoprotein from pig and the methylotrophic bacterium W3A1 contains AMP as well as FAD.

Author

DuPlessis ER, Rohlfs RJ, Hille R, and Thorpe C

Subjects
Adenosine Monophosphate analysis, Adenylate Kinase metabolism, Alkaline Phosphatase metabolism, Animals, Chromatography, High Pressure Liquid, Electron Transport, Flavin-Adenine Dinucleotide analysis, Kidney chemistry, Polymers, Spectrophotometry, Ultraviolet, Swine, Flavoproteins chemistry, Methylococcaceae chemistry
Abstract

Electron-transferring flavoproteins from pig kidney and from the methylotrophic bacterium W3A1 have been found to contain one molecule of AMP in addition to the single FAD molecule bound to these heterodimers. The nucleotide was identified by spectral and chromatographic methods and via its behavior toward adenylate kinase and alkaline phosphatase. The role of this additional non-redox active prosthetic group in electron transferring-flavoprotein is at present unclear.

Published
1994

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