Biotinylated peptides containing a factor XIIIa or a tissue transglutaminase-reactive glutaminyl residue that block protein cross-linking phenomena by becoming incorporated into amine donor sites

• Published in: Bioconjugate chemistry 1992-01, Vol.3 (1), p.37-41
• Main Authors: Lorand, L., Parameswaran, K. N., Velasco, P. T., Murthy, S. N. P.
• Format: Article
• Language: English
• Subjects: Amines - metabolism; Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Binding Sites; Biological and medical sciences; Biotin; Cross-Linking Reagents; Crystallins - chemistry; Crystallins - metabolism; Enzymes and enzyme inhibitors; Fibrin - chemistry; Fibrin - metabolism; Fundamental and applied biological sciences. Psychology; Glutamine - metabolism; Humans; Molecular Sequence Data; Peptides - chemistry; Peptides - metabolism; Transglutaminases - chemistry; Transglutaminases - metabolism
• ISSN: 1043-1802; 1520-4812
• DOI: 10.1021/bc00013a006

Biotinylated peptides Biot-Gln-Gln-Ile-Val and Biot-epsilon-Aca-Gln-Gln-Ile-Val were shown to act as acceptor substrates for amines in reactions catalyzed by both tissue transglutaminase and coagulation factor XIIIa. Moreover, the peptides could be employed for specifically blocking the potential amine donor sites of protein substrates participating in biological cross-linking with these enzymes. The presence of the biotin label allowed for ready detectability of the marked donor substrates during the cross-linking of crystallins in lens homogenate by the intrinsic transglutaminase and that of the alpha chains of human fibrin by factor XIIIa.