GTP modulates calcium binding and cation‐induced conformational changes in erythrocyte transglutaminase

FEBS Letters

Bergamini, Carlo M.¹ 

[1] Istituto di Chimica Biologica, Università di Ferrara, Via Borsari 46 44100 Ferrara, Italy

关键词: Transglutaminase;    Enzyme regulation;    GTP;    Ca2+ binding;    Proteolysis;    Fluorescence quenching;    (Human erythrocyte);   

DOI  :  10.1016/0014-5793(88)80928-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown