Premium
GTP modulates calcium binding and cation‐induced conformational changes in erythrocyte transglutaminase
Author(s) -
Bergamini Carlo M.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80928-1
Subject(s) - tissue transglutaminase , gtp' , chemistry , enzyme , calcium , biophysics , biochemistry , nucleotide , quenching (fluorescence) , conformational change , fluorescence , biology , organic chemistry , quantum mechanics , gene , physics
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.