ŽÍDEK, Lukáš, Petr DOLEŽEL, Josef CHMELÍK, Andrew G BAKER and Milos NOVOTNY. Modification of horse heart cytochrome c with trans-2-hexenal. Chemical Research in Toxicology. Washington, DC (USA): American Chemical Society, 1997, vol. 10, No 6, p. 702-710. ISSN 08993228X.
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Basic information
Original name Modification of horse heart cytochrome c with trans-2-hexenal
Authors ŽÍDEK, Lukáš, Petr DOLEŽEL, Josef CHMELÍK, Andrew G BAKER and Milos NOVOTNY.
Edition Chemical Research in Toxicology, Washington, DC (USA), American Chemical Society, 1997, 08993228X.
Other information
Type of outcome Article in a journal
Confidentiality degree is not subject to a state or trade secret
Organization unit Faculty of Science
Keywords in English ELECTROOSMOTIC ZONE DISPLACEMENT; LIPID-PEROXIDATION PRODUCTS; BOVINESERUM-ALBUMIN; PROTEIN ADDUCTS; ALDEHYDES
Tags ALDEHYDES, BOVINESERUM-ALBUMIN, ELECTROOSMOTIC ZONE DISPLACEMENT, LIPID-PEROXIDATION PRODUCTS, PROTEIN ADDUCTS
Changed by Changed by: prof. Mgr. Lukáš Žídek, Ph.D., učo 38990. Changed: 13/6/2001 09:43.
Abstract
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.
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