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  Purification and characterization of FAD synthetase from Brevibacterium ammoniagenes.

Manstein, D. J., & Pai, E. F. (1986). Purification and characterization of FAD synthetase from Brevibacterium ammoniagenes. The Journal of Biological Chemistry, 261(34), 16169-16173. Retrieved from https://www.jbc.org/content/261/34/16169.abstract.

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JBiolChem_261_1986_16169.pdf (Any fulltext), 2MB
 
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 Creators:
Manstein, Dietmar J.1, 2, Author              
Pai, Emil F.2, Author              
Affiliations:
1Dietmar Manstein Group, Max Planck Institute for Medical Research, Max Planck Society, ou_1497708              
2Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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 Abstract: The bifunctional enzyme FAD synthetase from Brevibacterium ammoniagenes was purified by a method involving ATP-affinity chromatography. The final preparation was more than 95% pure. The apparent molecular weight of the enzyme was determined as 38,000 and the isoelectric point as 4.6. Although previous attempts to separate the enzymatic activities had failed, ATP:riboflavin 5'-phosphotransferase and ATP:FMN-adenylyltransferase activities in B. ammoniagenes were believed to be located on two separate proteins with similar properties, possibly joined in a complex. The following evidence, however, suggests the presence of both activities on a single polypeptide chain. The two activities copurify in the same ratio through the purification scheme as presented. Only a single band could be detected when aliquots from the final purification step were subjected to sodium dodecyl sulfate-polyacrylamide gel electrophoresis, nondenaturing gel electrophoresis, and isoelectric focusing. Edman degradation of the protein yielded a single N-terminal sequence.

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Language(s): eng - English
 Dates: 1986-04-241986-12-05
 Publication Status: Published in print
 Pages: 5
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 Rev. Type: Peer
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Title: The Journal of Biological Chemistry
  Other : JBC
Source Genre: Journal
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Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: - Volume / Issue: 261 (34) Sequence Number: - Start / End Page: 16169 - 16173 Identifier: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826_1