Related Experiment Video
Updated: Jul 29, 2026
Expression of Recombinant Cellulase Cel5A from Trichoderma reesei in Tobacco Plants
Published on: June 13, 2014
[Characteristics of Triticale glutaminase]
L I Sidel'nikova1, Z G Evstigneeva, N A Solov'eva
1Bach Institute of Biochemistry, Russian Academy of Sciences, Leninskii pr. 33, Moscow, 117071 Russia.
Abstract:
The glutaminase (EC 3.5.1.2) isolated from seedlings of triticale (Triticale sp.) had a pH optimum of about 8, was inhibited with excess substrate (glutamine), and reaction products (glutamate and NH4+). A monovalent anion (Cl-) and a multivalent anion (phosphate) were shown to activate the glutaminase. Some features of the glutaminase from triticale were similar to those of animal glutaminase activated by phosphate and were different from features of the enzyme from Escherichia coli.
More Related Videos
08:01LERLIC-MS/MS for In-depth Characterization and Quantification of Glutamine and Asparagine Deamidation in Shotgun Proteomics
Published on: April 9, 2017
10:26Elucidating β-1,3-Glucanase and Peroxidase Physicochemical Properties of Wheat Cell Wall Defense Mechanism Against Diuraphis noxia Infestation
Published on: July 26, 2024