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Bulletin of the Korean Chemical Society (BKCS)

ISSN 0253-2964(Print)
ISSN 1229-5949(Online)
Volume 20, Number 11
BKCSDE 20(11)
November 20, 1999 

Investigation of Transglutaminase-Induced Peptide Cross-Linking by Matrix-Assisted
Hie-Joon Kim, Hyo Sup Yim
Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS) was used to demonstrate cross-linking of peptides induced by transglutaminase. The presence of ε-( Υ-glutamyl)lysine isopeptide cross-link in the acid hydrolysate of the cross-linking reaction mixture was also demonstrated by MALDI-TOF-MS without prior separation. MALDI-TOF-MS quickly provided peptide mass maps after pronase digestion of the cross-linked peptide adduct, which enabled us to monitor the hydrolytic sequence. Pronase appears to preferentially hydrolyze peptide bonds distant from the cross-link before hydrolyzing peptide bonds around the cross-link. The results suggest that pronase digestion followed by MALDI-TOF-MS could be used for determination of amino acid sequence around a modification site.
1299 - 1302
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