Interaction of erythrocyte transglutaminase with calcium ions.
We have investigated the interaction between calcium ions and erythrocyte transglutaminase and the enzyme activation. The binding involves both high and low affinity sites, but only the former ones are relevant for activation. The binding of calcium and the activation are modified by treatment with NBD-Cl and with PLP suggesting the presence of cysteine and lysine residues at the high affinity binding sites. The interaction of the enzyme with calcium is not calmodulin dependent and is easily detected as a shift in electrophoretic mobility in the presence of SDS.
Signorini
M
M
Istituto di Chimica Biologica dell'Università, Ferrara, Italy.
Chiozzi
P
P
Bergamini
C M
CM
D009327:4-Chloro-7-nitrobenzofurazan / Q000494:pharmacology; D001665:Binding Sites; D002118:Calcium / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D004912:Erythrocytes / Q000201:enzymology*; D011732:Pyridoxal Phosphate / Q000494:pharmacology; D011503:Transglutaminases / Q000037:antagonists & inhibitors / Q000378:metabolism*
D011732:Pyridoxal Phosphate; D011503:Transglutaminases; D009327:4-Chloro-7-nitrobenzofurazan; D002118:Calcium