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Reaction of Malonaldehyde with Protein
Author(s) -
CRAWFORD DAVID L.,
YU T. C.,
SINNHUBER RUSSELL O.
Publication year - 1967
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1967.tb01324_32_3.x
Subject(s) - chemistry , enamine , lysine , enol , amino acid , medicinal chemistry , nucleophile , reaction rate , reaction mechanism , kinetics , organic chemistry , biochemistry , catalysis , physics , quantum mechanics
SUMMARY— Malonaldehyde was shown to react with bovine plasma albumin under aqueous conditions by a pH‐dependent reaction exhibiting first‐order kinetics. The maximum reaction rate observed was near pH 4.30. The reaction was shown to involve the e‐amino lysine and N‐terminal amino aspartic acid groups on the protein as judged by their loss to reaction with 1‐fluoro‐2,4‐dinitrobenzene. Malonaldehyde did not appear to participate in an intermolecular cross‐linking reaction with gelatin sols over a wide pH range. Presumptive evidence was obtained for the reaction of malonaldehyde, derived from autoxidized lipid, with the c‐amino lysine functions on bovine plasma albumin. A nucleophilic 1,4‐addition of the free amino functions on the protein to the end carbon atom of the α,β‐unsaturated carbonyl system of the free enol of malonaldehyde to form an enamine linkage is postulated to be the mechanism for this reaction.