Literature DB >> 7651073

Determination of lysine modification product epsilon-N-pyrrolylnorleucine in hydrolyzed proteins and trout muscle microsomes by micellar electrokinetic capillary chromatography.

R Zamora1, J L Navarro, F J Hidalgo.   

Abstract

epsilon-N-Pyrrolylnorleucine (Pnl) is a product of the reaction between the lipid peroxidation product 4,5(E)-epoxy-2(E)-heptenal (EH) and the epsilon-amino group of lysine. Because Pnl might also be produced in proteins, a specific method to determine this compound in protein hydrolysates has been developed. Homoarginine, added as the internal standard, and Pnl are derivatized with diethyl ethoxymethylenemalonate and analyzed by micellar electrokinetic capillary chromatography. The method also analyzes lysine and arginine, and these analyses were useful in determining losses of these amino acids after treatment with EH. The lowest concentration of Pnl detected with acceptable reproducibility is 5 nmol/mL, and the coefficient of variation was determined from four standard curves assayed on separate days. Detector response was linear for samples containing 1.6 to 74 nmol/mL of Pnl. The assay was applied in investigations of Pnl production in bovine serum albumin (BSA) and trout muscle microsomes treated with EH. When BSA was incubated overnight with 30 mM EH, 76% of lysine residues were modified, and a part of these residues were detected as Pnl (12%). Pnl formation was also detected when trout muscle microsomes were incubated for three hours with 1 or 10 mM EH. These results show that Pnl is produced in vitro in proteins treated with the lipid peroxidation product EH, and suggest that Pnl might also be constituent of in vivo damaged proteins by their reaction with oxidized lipids.

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Year:  1995        PMID: 7651073     DOI: 10.1007/bf02537020

Source DB:  PubMed          Journal:  Lipids        ISSN: 0024-4201            Impact factor:   1.880


  8 in total

1.  Amino acid analysis by high-performance liquid chromatography after derivatization with diethyl ethoxymethylenemalonate.

Authors:  M Alaiz; J L Navarro; J Girón; E Vioque
Journal:  J Chromatogr       Date:  1992-02-07

2.  A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.

Authors:  M M Bradford
Journal:  Anal Biochem       Date:  1976-05-07       Impact factor: 3.365

3.  Lipid peroxidation damage to cell components.

Authors:  A L Tappel
Journal:  Fed Proc       Date:  1973-08

4.  Fluorescent pyrrole products from carbonyl-amine reactions.

Authors:  F J Hidalgo; R Zamora
Journal:  J Biol Chem       Date:  1993-08-05       Impact factor: 5.157

Review 5.  Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes.

Authors:  H Esterbauer; R J Schaur; H Zollner
Journal:  Free Radic Biol Med       Date:  1991       Impact factor: 7.376

6.  Release of ethane and pentane from rat tissue slices: effect of vitamin E, halogenated hydrocarbons, and iron overload.

Authors:  V C Gavino; C J Dillard; A L Tappel
Journal:  Arch Biochem Biophys       Date:  1984-09       Impact factor: 4.013

Review 7.  Lipid peroxidation: its mechanism, measurement, and significance.

Authors:  B Halliwell; S Chirico
Journal:  Am J Clin Nutr       Date:  1993-05       Impact factor: 7.045

Review 8.  Free radical-lipid interactions and their pathological consequences.

Authors:  C Rice-Evans; R Burdon
Journal:  Prog Lipid Res       Date:  1993       Impact factor: 16.195

  8 in total
  1 in total

1.  Lysine pyrrolation is a naturally-occurring covalent modification involved in the production of DNA mimic proteins.

Authors:  Hiroaki Miyashita; Miho Chikazawa; Natsuki Otaki; Yusuke Hioki; Yuki Shimozu; Fumie Nakashima; Takahiro Shibata; Yoshihisa Hagihara; Shoichi Maruyama; Noriyoshi Matsumi; Koji Uchida
Journal:  Sci Rep       Date:  2014-06-18       Impact factor: 4.379

  1 in total

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