Analysis of native human plasma proteins and haemoglobin for the presence of bityrosine by high-performance liquid chromatography
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Analysis of native human plasma proteins and haemoglobin for the presence of bityrosine by high-performance liquid chromatography. / Daneshvar, B; Frandsen, H; Dragsted, L O; Knudsen, Lisbeth E.; Autrup, H.
In: Pharmacology & Toxicology, Vol. 81, No. 5, 1997, p. 205-8.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Analysis of native human plasma proteins and haemoglobin for the presence of bityrosine by high-performance liquid chromatography
AU - Daneshvar, B
AU - Frandsen, H
AU - Dragsted, L O
AU - Knudsen, Lisbeth E.
AU - Autrup, H
N1 - Keywords: Adult; Air Pollution; Animals; Blood Proteins; Chromatography, High Pressure Liquid; Hemoglobins; Humans; Male; Middle Aged; Rabbits; Tyrosine
PY - 1997
Y1 - 1997
N2 - Generation of reactive oxygen species in vivo results in oxidative-damage to cellular components, including proteins. Due to the relatively long half-lives of several blood proteins the cumulative formation of oxidatively damaged proteins might serve as a biomarker for reactive oxygen species formation. The most prominent sources of reactive oxygen species in vivo are site-specific metal ion-catalyzed reactions of the Fenton and Haber-Weiss types and the H2O2/peroxidase system. In vitro oxidation of L-tyrosine using a peroxidase or Cu++/H2O2 system gives rise to the formation of a highly fluorescent substance, bityrosine. High-performance liquid chromatography (HPLC) analysis of acid hydrolyzed serum albumin after oxidation with peroxidase/H2O2 or with Cu++/H2O2 showed that bityrosine had been formed whereas oxidation of this protein with Fe(III)/ascorbate did not result in the formation of bityrosine. Bityrosine could not be detected in human plasma proteins or haemoglobin with the detection limit of one pmol per mg protein.
AB - Generation of reactive oxygen species in vivo results in oxidative-damage to cellular components, including proteins. Due to the relatively long half-lives of several blood proteins the cumulative formation of oxidatively damaged proteins might serve as a biomarker for reactive oxygen species formation. The most prominent sources of reactive oxygen species in vivo are site-specific metal ion-catalyzed reactions of the Fenton and Haber-Weiss types and the H2O2/peroxidase system. In vitro oxidation of L-tyrosine using a peroxidase or Cu++/H2O2 system gives rise to the formation of a highly fluorescent substance, bityrosine. High-performance liquid chromatography (HPLC) analysis of acid hydrolyzed serum albumin after oxidation with peroxidase/H2O2 or with Cu++/H2O2 showed that bityrosine had been formed whereas oxidation of this protein with Fe(III)/ascorbate did not result in the formation of bityrosine. Bityrosine could not be detected in human plasma proteins or haemoglobin with the detection limit of one pmol per mg protein.
M3 - Journal article
C2 - 9396084
VL - 81
SP - 205
EP - 208
JO - Pharmacology and Toxicology
JF - Pharmacology and Toxicology
SN - 0901-9928
IS - 5
ER -
ID: 19231982