Conformational stability of human erythrocyte transglutaminase.

Autor: Bergamini, Carlo M., Dean, Mariangela, Matteucci, Gabriella, Hanau, Stefani, Tanfani, Fabio, Ferrari, Carlo, Boggian, Marisa, Scatturin, Angelo
Předmět:
Zdroj: European Journal of Biochemistry; Dec99 Part 1, Vol. 266 Issue 2, p575, 8p, 3 Diagrams, 12 Graphs
Abstrakt: Examines the conformational stability of human erythrocyte transglutaminase. Inactivation rate of the hydrogen-ion concentration; Use of differential scanning calorimetry in thermal unfolding of protein; Effects of pH; Ionization of state of crucial lysine residues.
Databáze: Complementary Index