[Study of different conformational states of transketolase by the method of perturbation UV-spectrophotometry].
The conformational parameters of apotransketolase, holotransketolase and the enzyme-substrate complex were studied using colvent perturbation technique, a 20% solution of dimethyl sulfoxide being used as perturbant. The apoenzyme was found to contain 4--5 tryptophane residues and 12--14 tyrosine residues accessible for the solvent. The amount of the residues is reduced nearly 2-fold after formation of the holoenzyme. In the enzyme-substrate complex the amount of tryptophane and tyrosine residues accessible for the solvent is increased up to the inital value. The changes in the conformational states of the active site of apoenzyme, holoenzyme and the enzyme-substrate complex are discussed.
D000817:Anilino Naphthalenesulfonates; D001051:Apoenzymes; D055598:Chemical Phenomena; D002621:Chemistry; D011487:Protein Conformation; D013056:Spectrophotometry, Ultraviolet; D014174:Transketolase
D000817:Anilino Naphthalenesulfonates; D001051:Apoenzymes; D014174:Transketolase
Izuchenie razlichnykh konformatsionnykh sostoianiĭ transketolazy metodom perturbatsionnoĭ UF-spektrofotometrii.