Bergamini C M
Istituto di Chimica Biologica, Università di Ferrara, Italy.
FEBS Lett. 1988 Nov 7;239(2):255-8. doi: 10.1016/0014-5793(88)80928-1.
Calcium binding to erythrocyte transglutaminase was determined by equilibrium dialysis. Results indicate that 6 ions are bound to the enzyme both in the absence and in the presence of GTP and that the nucleotide reduces the affinity of the enzyme for calcium. Furthermore, I- fluorescence quenching and proteolytic inactivation experiments proved that GTP also alters the conformation of the enzyme. It is thus suggested that multiple mechanisms are involved in the regulation of the enzyme activity by GTP.
通过平衡透析法测定钙与红细胞转谷氨酰胺酶的结合情况。结果表明，在不存在和存在GTP的情况下，均有6个离子与该酶结合，并且核苷酸降低了该酶对钙的亲和力。此外，碘荧光猝灭和蛋白水解失活实验证明，GTP也会改变该酶的构象。因此，提示GTP通过多种机制参与该酶活性的调节。
