Modification of horse heart cytochrome c with trans-2-hexenal

ŽÍDEK, Lukáš, Petr DOLEŽEL, Josef CHMELÍK, Andrew G BAKER a Milos NOVOTNY. Modification of horse heart cytochrome c with trans-2-hexenal. Chemical Research in Toxicology. Washington, DC (USA): American Chemical Society, 1997, roč. 10, č. 6, s. 702-710. ISSN 08993228X.

Základní údaje

Originální název

Modification of horse heart cytochrome c with trans-2-hexenal

Autoři

ŽÍDEK, Lukáš, Petr DOLEŽEL, Josef CHMELÍK, Andrew G BAKER a Milos NOVOTNY

Vydání

Chemical Research in Toxicology, Washington, DC (USA), American Chemical Society, 1997, 08993228X

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Další údaje

Typ výsledku

Článek v odborném periodiku

Utajení

není předmětem státního či obchodního tajemství

Organizační jednotka

Přírodovědecká fakulta

Klíčová slova anglicky

ELECTROOSMOTIC ZONE DISPLACEMENT; LIPID-PEROXIDATION PRODUCTS; BOVINESERUM-ALBUMIN; PROTEIN ADDUCTS; ALDEHYDES

Štítky

ALDEHYDES, BOVINESERUM-ALBUMIN, ELECTROOSMOTIC ZONE DISPLACEMENT, LIPID-PEROXIDATION PRODUCTS, PROTEIN ADDUCTS

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Anotace

V originále

Horse heart cytochrome c reacting with trans-2-hexenal was used as a simple model of the nonspecific interactions of proteins with 2-alkenals. The reaction mixtures containing relatively high concentrations of the protein and aldehyde were characterized using visible spectrophotometry, fluorescence, and circular dichroism measurements, capillary isoelectric focusing, size-exclusion chromatography, polyacrylamide gel electrophoresis, and mass-spectrometric techniques. The mass-spectrometric data indicate that cytochrome c becomes modified with one or two molecules of hexenal as the major reaction product. The modified species with a correspondingly lowered isoelectric point were detected through capillary isoelectric focusing. The results of proteolytic studies indicate nonspecific modifications. Significant quantities of the oligomeric farms of hexenal-modified protein were also observed electrophoretically.