Transglutaminase-catalyzed polymerization of troponin in vitro.
In the presence of calcium ions, tissue transglutaminase catalyzes the polymerization of skeletal muscle troponin to high molecular weight insoluble aggregate. The specific action of transglutaminase is proved by the isolation of glutamyl-spermidine isopeptide derivatives. The process involves mainly the troponin T subunit (TnT), with formation of dimers and trimers of TnT, which were reactive with specific antibodies by immunoblotting. Furthermore when incubation is carried out in the presence of radioactive polyamines, the label is incorporated selectively into TnT subunits.
Bergamini
C M
CM
Department of Biochemistry and Molecular Biology, University of Ferrara, Italy.
Signorini
M
M
Barbato
R
R
Menabò
R
R
Di Lisa
F
F
Gorza
L
L
Beninati
S
S
D000818:Animals; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D004912:Erythrocytes / Q000201:enzymology; D006801:Humans; D046911:Macromolecular Substances; D008970:Molecular Weight; D018482:Muscle, Skeletal / Q000378:metabolism; D011817:Rabbits; D013095:Spermidine / Q000378:metabolism; D011503:Transglutaminases / Q000302:isolation & purification / Q000378:metabolism*; D014336:Troponin / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*
D046911:Macromolecular Substances; D014336:Troponin; D011503:Transglutaminases; D013095:Spermidine