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. 1995 Apr 15;307(Pt 2):331–333. doi: 10.1042/bj3070331

Levels of pyrroloquinoline quinone in various foods.

T Kumazawa 1, K Sato 1, H Seno 1, A Ishii 1, O Suzuki 1
PMCID: PMC1136652  PMID: 7733865

Abstract

The levels of free pyrroloquinoline quinone (PQQ) in various foods were examined by the use of gas chromatography-mass spectrometry. PQQ was extracted from the samples, after addition of [U-13C]PQQ as internal standard, with n-butanol and Sep-Pak C18 cartridges. After derivatization of PQQ with phenyltrimethylammonium hydroxide, molecular peaks at m/z 448 and 462 were used for detection of PQQ and [U-13C]PQQ respectively, by selected ion monitoring. Free PQQ could be detected in every sample in the range 3.7-61 ng/g or ng/ml. Since its levels in human tissues and body fluids are 5-10 times lower than those found in foods, it is probable that PQQ existing in human tissues is derived, at least partly, from the diet.

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Selected References

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  1. Groen B. W., van der Meer R. A., Duine J. A. Evidence for PQQ as cofactor in 3,4-dihydroxyphenylalanine (dopa) decarboxylase of pig kidney. FEBS Lett. 1988 Sep 12;237(1-2):98–102. doi: 10.1016/0014-5793(88)80179-0. [DOI] [PubMed] [Google Scholar]
  2. Hamagishi Y., Murata S., Kamei H., Oki T., Adachi O., Ameyama M. New biological properties of pyrroloquinoline quinone and its related compounds: inhibition of chemiluminescence, lipid peroxidation and rat paw edema. J Pharmacol Exp Ther. 1990 Dec;255(3):980–985. [PubMed] [Google Scholar]
  3. Janes S. M., Mu D., Wemmer D., Smith A. J., Kaur S., Maltby D., Burlingame A. L., Klinman J. P. A new redox cofactor in eukaryotic enzymes: 6-hydroxydopa at the active site of bovine serum amine oxidase. Science. 1990 May 25;248(4958):981–987. doi: 10.1126/science.2111581. [DOI] [PubMed] [Google Scholar]
  4. Killgore J., Smidt C., Duich L., Romero-Chapman N., Tinker D., Reiser K., Melko M., Hyde D., Rucker R. B. Nutritional importance of pyrroloquinoline quinone. Science. 1989 Aug 25;245(4920):850–852. doi: 10.1126/science.2549636. [DOI] [PubMed] [Google Scholar]
  5. Kumazawa T., Seno H., Suzuki O. Failure to verify high levels of pyrroloquinoline quinone in eggs and skim milk. Biochem Biophys Res Commun. 1993 May 28;193(1):1–5. doi: 10.1006/bbrc.1993.1581. [DOI] [PubMed] [Google Scholar]
  6. Kumazawa T., Seno H., Urakami T., Suzuki O. Failure to verify the presence of pyrroloquinoline quinone (PQQ) in bovine plasma amine oxidase by gas chromatography/mass spectrometry. Arch Biochem Biophys. 1990 Dec;283(2):533–536. doi: 10.1016/0003-9861(90)90679-s. [DOI] [PubMed] [Google Scholar]
  7. Lobenstein-Verbeek C. L., Jongejan J. A., Frank J., Duine J. A. Bovine serum amine oxidase: a mammalian enzyme having covalently bound PQQ as prosthetic group. FEBS Lett. 1984 May 21;170(2):305–309. doi: 10.1016/0014-5793(84)81333-2. [DOI] [PubMed] [Google Scholar]
  8. Mincey T., Bell J. A., Mildvan A. S., Abeles R. H. Mechanism of action of methoxatin-dependent alcohol dehydrogenase. Biochemistry. 1981 Dec 22;20(26):7502–7509. doi: 10.1021/bi00529a027. [DOI] [PubMed] [Google Scholar]
  9. Moog R. S., McGuirl M. A., Cote C. E., Dooley D. M. Evidence for methoxatin (pyrroloquinolinequinone) as the cofactor in bovine plasma amine oxidase from resonance Raman spectroscopy. Proc Natl Acad Sci U S A. 1986 Nov;83(22):8435–8439. doi: 10.1073/pnas.83.22.8435. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Naito Y., Kumazawa T., Kino I., Suzuki O. Effects of pyrroloquinoline quinone (PQQ) and PQQ-oxazole on DNA synthesis of cultured human fibroblasts. Life Sci. 1993;52(24):1909–1915. doi: 10.1016/0024-3205(93)90631-c. [DOI] [PubMed] [Google Scholar]
  11. Nishigori H., Yasunaga M., Mizumura M., Lee J. W., Iwatsuru M. Preventive effects of pyrroloquinoline quinone on formation of cataract and decline of lenticular and hepatic glutathione of developing chick embryo after glucocorticoid treatment. Life Sci. 1989;45(7):593–598. doi: 10.1016/0024-3205(89)90044-1. [DOI] [PubMed] [Google Scholar]
  12. Paz M. A., Flückiger R., Torrelio B. M., Gallop P. M. Methoxatin (PQQ), coenzyme for copper-dependent amine and mixed-function oxidation in mammalian tissues. Connect Tissue Res. 1989;20(1-4):251–257. doi: 10.3109/03008208909023895. [DOI] [PubMed] [Google Scholar]
  13. Robertson J. G., Kumar A., Mancewicz J. A., Villafranca J. J. Spectral studies of bovine dopamine beta-hydroxylase. Absence of covalently bound pyrroloquinoline quinone. J Biol Chem. 1989 Nov 25;264(33):19916–19921. [PubMed] [Google Scholar]
  14. Salisbury S. A., Forrest H. S., Cruse W. B., Kennard O. A novel coenzyme from bacterial primary alcohol dehydrogenases. Nature. 1979 Aug 30;280(5725):843–844. doi: 10.1038/280843a0. [DOI] [PubMed] [Google Scholar]
  15. Steinberg F. M., Gershwin M. E., Rucker R. B. Dietary pyrroloquinoline quinone: growth and immune response in BALB/c mice. J Nutr. 1994 May;124(5):744–753. doi: 10.1093/jn/124.5.744. [DOI] [PubMed] [Google Scholar]
  16. van der Meer R. A., Duine J. A. Covalently bound pyrroloquinoline quinone is the organic prosthetic group in human placental lysyl oxidase. Biochem J. 1986 Nov 1;239(3):789–791. doi: 10.1042/bj2390789. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. van der Meer R. A., Jongejan J. A., Duine J. A. Dopamine beta-hydroxylase from bovine adrenal medulla contains covalently-bound pyrroloquinoline quinone. FEBS Lett. 1988 Apr 25;231(2):303–307. doi: 10.1016/0014-5793(88)80838-x. [DOI] [PubMed] [Google Scholar]
  18. van der Meer R. A., Jongejan J. A., Frank J., Duine J. A. Hydrazone formation of 2,4-dinitrophenylhydrazine with pyrroloquinoline quinone in porcine kidney diamine oxidase. FEBS Lett. 1986 Sep 29;206(1):111–114. doi: 10.1016/0014-5793(86)81350-3. [DOI] [PubMed] [Google Scholar]

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