Peroxidase induced oligo-tyrosine cross-links during polymerization of α-lactalbumin.
作者： Surender Kumar Dhayal , Stefano Sforza , Peter A. Wierenga , Harry Gruppen
DOI: 10.1016/J.BBAPAP.2015.08.001
关键词:
摘要: Horseradish peroxidase (HRP) induced cross-linking of proteins has been reported to proceed through formation di-tyrosine cross-links. In the case low molar mass phenolic substrates, enzymatic oxidation is lead polymerization phenols. The aim this work was investigate if during oxidative oligo-tyrosine cross-links are formed in addition dityrosine. To end, α-lactalbumin (α-LA) cross-linked using horseradish and hydrogen peroxide (H₂O₂). reaction products were acid hydrolysed, after which amino acids investigated by LC-MS MALDI-MS. test effect size substrate, also performed with L-tyrosine, N-acetyl L-tyrosinamide angiotensin. These analyzed directly, as well hydrolysis. hydrolysates all samples (Yn, n=3-8) found (Y2). Two stages α-LA identified: a) 1-2 per monomer until monomers converted into oligomers, b) subsequent oligomers first stage form nanoparticles containing 3-4 monomer. transition from second coincided point where started decrease more oligo-tyrosines formed. conclusion, extensive HRP via possible, for tyrosine substrates.
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