The Biosynthesis of Riboflavin: Affinity Chromatography Purification of GTP-Ring-Opening Enzyme

  • L. Preston Mercer
  • Charles M. Baugh
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 42)


The ability of guanine compounds to serve as precursors of riboflavin has been well established (1,2). This ability was demonstrated in two different organisms in which purine-purine interconversions were blocked to insure retention of radioactive label in the specified molecule. The direct participation of the ribosyl moiety of a guanine nucleoside or nucleotide has not been established. The observation that loss of carbon 8 of guanine precedes riboflavin biosynthesis has led to its comparison with pteridine biosynthesis, which has a similar beginning (3,4). While the ribose moiety of GTP has been shown to be incorporated into pteridines (5) it does not appear to be directly incorporated as the ribityl side chain of riboflavin (6). Therefore, it is not known whether expulsion of carbon 8 of the imidazole portion of GTP represents a common first step in the biosynthesis of both vitamins or the initiation of two independent but similar pathways. (Figure 1.)


Cyanogen Bromide Amino Caproic Acid Guanosine Triphosphate Ribose Moiety Affinity Chromatography Purification 
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Copyright information

© Plenum Press, New York 1974

Authors and Affiliations

  • L. Preston Mercer
    • 1
  • Charles M. Baugh
    • 1
  1. 1.Department of BiochemistryUniversity of South Alabama, College of MedicineMobileUSA

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