Modification of different IgG1 antibodies via glutamine and lysine using bacterial and human tissue transglutaminase

Bioconjugate Chemistry

Volumn 19, Issue 1, 2008, Pages 271-278

  Mindt, Thomas L ^a   Jungi, Vera ^a   Wyss, Sara ^a   Friedli, Alexandra ^b   Pla, Gloria ^c   Novak Hofer, Ilse ^b   Grünberg, Jürgen ^b   Schibli, Roger ^a,b,d  

^a ETH ZURICH   (Switzerland)

^b ETH Zurich   (Switzerland)

^c UNIVERSITY OF BARCELONA   (Spain)

^d Center for Radiopharmaceutical Science ETH PSI USZ

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ANTIBODIES; CHAINS; CHEMICAL MODIFICATION; ENZYMES; TISSUE;

CHEMICAL METHOD; ENZYMATIC METHODS; FUNCTIONALIZATIONS; HUMAN TISSUES; LABELINGS; OPTIMAL REACTION CONDITION; POST-TRANSLATIONAL MODIFICATIONS; PROOF OF CONCEPT; SIDE-CHAINS; TISSUE TRANSGLUTAMINASE;

SUBSTRATES;

BENZYLOXYCARBONYLGLUTAMINYLGLUTAMINYLPROLYLLEUCYL CADAVARINE DY 547; BENZYLOXYCARBONYLGLUTAMINYLGLYCYL CADAVARINE DY 547; CADAVARINE DY 547; CELL ADHESION MOLECULE; CELL ADHESION MOLECULE L1; CY 3; FLUORESCENT DYE; GLUTAMINE; IMMUNOGLOBULIN G1 ANTIBODY; LYSINE; MONOCLONAL ANTIBODY CHCE7; PEPTIDE DERIVATIVE; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; UNCLASSIFIED DRUG;

ANTIBODY AFFINITY; ARTICLE; CATALYSIS; CATALYST; CONFOCAL LASER MICROSCOPY; ENZYME ACTIVITY; ENZYME SUBSTRATE COMPLEX; FLUORESCENCE; HUMAN; HUMAN CELL; INTERMETHOD COMPARISON; INTERNALIZATION; NONHUMAN; PROTEIN PROCESSING; REACTION ANALYSIS; SYNTHESIS;

BACTERIA (MICROORGANISMS); BOVINAE;

EID: 38949104404     PISSN: 10431802     EISSN: None     Source Type: Journal    
DOI: 10.1021/bc700306n     Document Type: Article

References (29)

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25. Initially, the antibody labeling experiments were conducted with similar results using BTGase and commercial cadavarinedansyl and ZGlnGly cadavarine-dansyl substrates. However, the dansyl fluorophore proved to be unsuitable for fluorescence microscopy of cell samples.
26. Similar results were obtained with commercial human and chicken IgG.
27. Interestingly, Josten et al. have reported a labeling degree of 1.1 to 1.4 labels per antibody for the BTGase-mediated biotinylation of a monoclonal IgG using a Lys-substrate (11).
28. For example, storage of solutions of TG2 on ice for 1 h resulted in a decrease of the enzyme's activity by 50% (data not shown, loss of activity of mammalian TGases has previously been reported by Jeitner et al. (20)). No loss of activity was observed for BTGase even after storage of solutions at it for several hours.
29. Josten et al. (11) and Takazawa et al. (72) also report unaltered antigen binding of antibodies and antibody fragments that were modified by TGases.