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 mainl...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 1995-01, Vol.206 (1), p.201-206
Main Authors: Bergamini, C.M., Signorini, M., Barbato, R., Menabo, R., Dilisa, F., Gorza, L., Beninati, S.
Format: Article
Language:English
Subjects:
Animals
Chromatography, Affinity
Electrophoresis, Polyacrylamide Gel
Erythrocytes - enzymology
Humans
Macromolecular Substances
Molecular Weight
Muscle, Skeletal - metabolism
Rabbits
Spermidine - metabolism
Transglutaminases - isolation & purification
Transglutaminases - metabolism
Troponin - chemistry
Troponin - isolation & purification
Troponin - metabolism
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Description
Summary: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.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1995.1028