Lipid oxidation induced by oxymyoglobin and metmyoglobin with involvement of H(2)O(2) and superoxide anion

Autor:	Cameron Faustman, M. Yin, Eric A. Decker, Wendy K. M. Chan
Rok vydání:	1996
Předmět:	Liposome Antioxidant Superoxide medicine.medical_treatment Albumin Biological activity Photochemistry chemistry.chemical_compound Metmyoglobin Myoglobin chemistry Lipid oxidation Biochemistry medicine lipids (amino acids peptides and proteins) Food Science
Zdroj:	Meat science. 46(2)
ISSN:	0309-1740
Popis:	The role of oxymyoglobin oxidation in lipid oxidation was studied in a myoglobin-liposome system. The pro-oxidant effect of oxymyoglobin towards lipid oxidation was concentration-dependent. At equimolar concentrations, oxymyoglobin showed higher pro-oxidative activity towards lipid than metmyoglobin (p0.05). These results suggested that the process of oxymyoglobin oxidation is involved in catalyzing lipid oxidation. The addition of catalase into the oxymyoglobin-liposome system resulted in significantly decreased oxidation of oxymyoglobin and lipid (p0.05) suggesting a role for H(2)O(2) in the interaction between oxymyoglobin and lipid. The addition of Superoxide dismutase was without effect (p0.05) suggesting that Superoxide anion was not directly involved in mediating oxidation of oxymyoglobin and lipid. Albumin was added as a control for a non-specific protein antioxidant; it did not affect oxymyoglobin or lipid oxidation (p0.05). Our in vitro results support the hypothesis that the actual process of oxymyoglobin oxidation is a catalyst of lipid oxidation with H(2)O(2) a major factor.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::880a0185406184efb5a801ed056bb1d1 https://pubmed.ncbi.nlm.nih.gov/22062041 Zobrazit plný text záznamu Full Text from ScienceDirect