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Redox Report
Communications in Free Radical Research
Volume 1, 1995 - Issue 4
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Original Articles

A sensitive fluorometric assay for protein-bound DOPA and related products of radical-mediated protein oxidation

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Pages 291-298 | Accepted 17 Mar 1995, Published online: 13 Jul 2016

References

  • Simpson J A, Narita S, Gieseg S, Gebicki S, Gebicki J M, Dean R T. Long-lived reactive species on free-radical-damage proteins. Biochem J 1992; 282: 621–624.
  • Gieseg S P, Simpson J A, Charlton T S, Duncan M W, Dean R T. Protein-bound 3,4-dihydroxyphenylalanine is a major reductant formed during hydroxyl radical damage to proteins. Biochemistry 1993; 32: 4780–4786.
  • Dean R T, Gieseg S, Davies M J. Reactive species and their accumulation on radical-damaged proteins. Trends Biochem Sci 1993; 18: 437–441.
  • Simpson J A, Gieseg S P, Dean R T. Free radical and enzymatic mechanisms for the generation of protein bound reducing moieties. Biochim Biophys Acta 1993; 1156: 190–196.
  • Waite J H. The phylogeny and chemical diversity of quinonetanned glues and varnishes. Comp Biochem Physiol 1990; 97B: 19–29.
  • Huggins L G, Waite J H. Eggshell formation in Bdelloura candida, an ectoparasitic turbellarian of the horeshoe crab limulus polyphemus. J Exp Zool 1993; 265: 549–557.
  • Waite J H. Determination of (catecholato) borate complexes using difference spectrophotometry. Anal Chem 1984; 56: 1935–1939.
  • Waite J H, Tanzer M L. Specific colorimetric detection of odiphenols and 3,4-dihydroxyphenylalanine-containing peptides. Anal Biochem 1981; 111: 131–136.
  • Natelson S, Lugovoy J K, Pincus J B. A new fiuorometric method for the determination of epinephrine. Arch Biochem Biophys 1949; 23: 157–158.
  • Weil-Malherbe H, Bone A D. A chemical estimation of adrenaline-like substances in blood. Biochem J 1952; 51: 311–318.
  • Mori K, Imai K. Sensitive high-performance liquid chromatography system with fiuorometric detection of three urinary catecholamines in the same range. Anal Biochem 1985; 146: 283–286.
  • Waite J H, Saleuddin A S M, Andersen S O. Periostracin—a soluble precursor of sclerotized periostracum in Mytilus edulis L. J Comp Physiol 1979; 130: 301–307.
  • Ito S, Kato T, Shinpo K, Fujita K. Oxidation of tyrosine residues in proteins by tyrosinase- formation of protein-bonded 3,4-dihydroxyphenylalanine and 5-S-cysteinyl-3,4-dihydroxyphenylalanine. Biochem J 1984; 222: 407–411.
  • Yagi K, Nagatsu T. Condensation products of ethylenediamine with catechol derivatives. J Biochem 1960; 48: 439–452.
  • Yagi K, Nagatsu T, Nagatsu-Ishibashi I. Condensation reaction of DOPA with ethylenediamine. J Biochem 1960; 48(4): 617–620.
  • Rzepecki L M, Nagafuchi T, Waite J H. α,β-Dehydro-3,4-dihydroxyphenylalanine derivatives: potential schlerotization intermediates in natural composite materials. Arch Biochem Biophys 1991; 285: 17–26.
  • Rzepecki L M, Waite J H. α, beta;-Dehydro-3,4-dihydroxyphenylalanine derivatives: rate and mechanism of formation. Arch Biochem Biophys 1991; 285: 27–36.
  • Mcintire W S, Wemmer D E, Chistoserdov A, Lidstrom M E. A new cofactor in a prokaryotic enzyme: tryptophan tryptophylquinone as the redox prosthetic group in methylamine dehydrogenase. Science. 252(5007); 817–824.
  • Chen L Y, Mathews F S, Davidson V L et al. Crystallographic investigations of the tryptophan-derived cofactor in the quinoprotein methylamine dehydrogenase. FEBS Lett 1991; 287: 163–166.
  • Cox D D, Benkovic S J, Bloom L M et al. Catecholate LMCT bands as probes for the active sites of nonheme iron oxygenases. J Am Chem Soc 1988; 110: 2026–2032.
  • Andersson K K, Cox D D, Que Jr L, Flatmark T, Haavik J. Resonance Raman studies on the blue-green-colorec bovine adrenal tyrosine 3-monooxygenase (Tyrosine Hydroxylase). J Biol Chem 1988; 263: 18621–18626.
  • Ormo M, deMare F, Regnstrom K et al. Engineering of the iron site in ribonucleotide reductase to a self-hydroxylating monooxygenase. J Biol Chem. 1992; 267: 8711–8714.
  • Lowry O H, Rosebrough N J, Farr A L, Randall R J. Protein measurement with the folin phenol reagent. J Biol Chem 1951; 193: 265–274.

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