PMID: 3730052Jul 1, 1986

The biochemistry of epsilon-amino groups of lysine residues from apolipoprotein B of human low density lipoprotein

E Cocuzzi, W C Breckenridge


The availability of epsilon-lysine residues of apolipoprotein B in LDL for chemical or enzymic modification was investigated. Amino acid analyses of detergent-solubilized apolipoprotein B, following cyanoethylation with acrylonitrile, revealed that 10% of the lysine in apolipoprotein B were unreactive. The unreactive residues were associated with the most hydrophobic subfraction of apolipoprotein B. Since apolipoprotein B has a high molecular weight a study was undertaken to determine whether lysine residues were crosslinked to glutamic acid via epsilon-(gamma-glutamyl)lysine as demonstrated for fibrin. Apolipoprotein B was digested exhaustively with proteases. The content of epsilon-(gamma-glutamyl) lysine was determined by chromatography and isotope dilution. In contrast to earlier reports for serum LDL the data showed that less than 0.01 moles of lysine/mole of LDL apolipoprotein B were present as epsilon-(gamma-glutamyl)lysine in plasma LDL. It was determined also that the crosslinks were not found in apolipoprotein B during clotting since LDL was not a substrate for clotting factor XIII which forms the bond in fibrin. Furthermore, the lipoprotein contained no inherent transglutaminase activity. It is concluded that the lys...Continue Reading


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