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.
Publication types
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adenosine Monophosphate / analysis
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Adenylate Kinase / metabolism
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Alkaline Phosphatase / metabolism
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Animals
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Chromatography, High Pressure Liquid
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Electron Transport
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Flavin-Adenine Dinucleotide / analysis
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Flavoproteins / chemistry*
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Kidney / chemistry
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Methylococcaceae / chemistry*
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Polymers
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Spectrophotometry, Ultraviolet
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Swine
Substances
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Flavoproteins
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Polymers
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Flavin-Adenine Dinucleotide
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Adenosine Monophosphate
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Adenylate Kinase
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Alkaline Phosphatase