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  • Title: Myeloperoxidase-catalyzed binding of 3-amino-1-methyl-5H-pyrido[4,3-b]indole, a tryptophan pyrolysis product, to protein.
    Author: Yamada M, Mori M, Sugimura T.
    Journal: Chem Biol Interact; 1980 Dec; 33(1):19-33. PubMed ID: 6254679.
    Abstract:
    Incorporation of 3-amino-1-methyl-5H-pyrido[4,3-b]indole (Trp-P-2), the principal mutagen in a tryptophan pyrolysate, into bovine serum albumin was catalyzed by myeloperoxidase. Hydrogen peroxide was essential for the incorporation reaction and albumin was required for optimal incorporation of Trp-P-2 into protein. Other various proteins, such as histone, lysozyme, cytochrome c, and gamma-globulin could also incorporate Trp-P-2, but poly(L-Arg), poly(L-Lys), and poly(L-Glu) could not. The incorporation of Trp-P-2 into albumin was inhibited by L-tyrosine and L-tryptophan, but not by other amino acids. Trp-P-2 incorporated into albumin was not released from the protein by treatment with 0.3 N HCl, or 0.3 N NaOH for 2 h at 35 degrees C, or with 1% sodium dodecylsulfate for 2.5 min at 100 degrees C. On electrophoresis on polyacrylamide containing sodium dodecylsulfate or urea and on chromatography on Sepharose CL-6B in 6 M guanidine/HCl, Trp-P-2 incorporated into albumin or lysozyme migrated with these proteins. These findings indicate that Trp-P-2 is covalently bound to these acceptor proteins.
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