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.
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.
Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, Illinois 60208.
L
L
Lorand
K N
KN
Parameswaran
P T
PT
Velasco
S N
SN
Murthy
D000588:Amines / Q000378:metabolism; D000595:Amino Acid Sequence; D001665:Binding Sites; D001710:Biotin; D003432:Cross-Linking Reagents; D003459:Crystallins / Q000737:chemistry / Q000378:metabolism; D005337:Fibrin / Q000737:chemistry / Q000378:metabolism; D005973:Glutamine / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry / Q000378:metabolism*; D011503:Transglutaminases / Q000737:chemistry / Q000378:metabolism*
D000588:Amines; D003432:Cross-Linking Reagents; D003459:Crystallins; D010455:Peptides; D005973:Glutamine; D001710:Biotin; D005337:Fibrin; D011503:Transglutaminases