Beyond Dinitrophenol Interaction with Tryptophan-Based Compounds

Sn(IV) Compounds Interaction with Metal-Schiff Base Complexes

The formation constants and Gibbs free energy for the interaction of RnSnClm (n = m = 2, R = Me, Ph, n-Bu or n = 4, m = 0, R = Ph) compounds as acceptors, with ML complexes (H2L = N,N'-bis(salicylidene)-2-aminobenzylamine (salabza-H2) and its derivatives, M = Mn2+ or Zn2+), as donors in N,N'-dimethylformamide (DMF) as solvent were studied. These parameters were measured by using UV-vis spectrop...

Tryptophan Catabolism in Cancer: Beyond IDO and Tryptophan

Tryptophan catabolism in cancer is increasingly being recognized as an important microenvironmental factor that suppresses antitumor immune responses. It has been proposed that the essential amino acid tryptophan is catabolized in the tumor tissue by the rate-limiting enzyme indoleamine-2,3-dioxygenase (IDO) expressed in tumor cells or antigen-presenting cells. This metabolic pathway creates an...

Tryptophan catabolism in cancer: beyond IDO and tryptophan depletion.

Tryptophan catabolism in cancer is increasingly being recognized as an important microenvironmental factor that suppresses antitumor immune responses. It has been proposed that the essential amino acid tryptophan is catabolized in the tumor tissue by the rate-limiting enzyme indoleamine-2,3-dioxygenase (IDO) expressed in tumor cells or antigen-presenting cells. This metabolic pathway creates an...

The oxidation of tryptophan and some related compounds with persulphate.

Effect of dinitrophenol on the interaction between myosin and nucleotides.

Webster (1) first noticed that 2,4-dinitrophenol increased the ATPase” activity of myosin. Attention was focused on this observation by the work of Greville and Needham (2) and Chappell and Perry (3), who showed that under certain conditions DNP accelerated the ATPase activity of myosin A, myosin B, and myofibrils, whereas the ITPase activity was inhibited. They noted the similarity between the...