Abstract
We have found that PQQ can be directly measured with 3-methyl-2-ben-zothiazolinone hydrazone. PQQ can also be specifically detected with much greater sensitivity by its unique ability to support redox cycling. A reagent prepared from potassium glycinate and nitroblue tetrazolium can lead to the formation of amplified levels of formazan dye in the presence of picomoles of PQQ. Confirmation of PQQ as the coenzyme in pig kidney diamine oxidase and bovine adrenal dopamine-β-hydroxylase is presented with isolation of PQQ-peptides from pronase digests of these quinoenzymes. PQQ is also present in trace levels in some proteins and completely absent from others. It is present in serum, CSF, urine, milk and egg-yolk. The concentration of PQQ in biological fluids may have clinical and pathophysiological significance. Reduced PQQ generates superoxide with oxygen and has the potential to become a source of oxidative stress in damaged tissues and to contribute to inflammatory processes.
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© 1989 Kluwer Academic Publishers
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Paz, M.A., Flückiger, R., Henson, E., Gallop, P.M. (1989). Direct and Amplified Redox-Cycling Measurements of PQQ in Quinofroteins and Biological Fluids: PQQ-Peptides in Pronase Digests of DBH and DAO. In: Jongejan, J.A., Duine, J.A. (eds) PQQ and Quinoproteins. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-0957-1_20
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DOI: https://doi.org/10.1007/978-94-009-0957-1_20
Publisher Name: Springer, Dordrecht
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