Effect of human neuronal tau on denaturation and reactivation of rabbit muscle D-glyceraldehyde-3-phosphate dehydrogenase.

REASSOCIATION AND REACTIVATION OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM STREPTOMYCES AUREOFACIENS AFTER DENATURATION BY 6 M UREA

Glucose 6-phosphate dehydrogenase (G6PD) from Streptomyces aureofaciens was purified and denatured in 6 M urea. Denaturation led to complete dissociation of the enzyme into its inactive monomers, 98% loss of the enzyme activity, about 30% decrease in the protein fluorescence and a 10 nm red shift in the emission maximum. Dilution of urea-denatured enzyme resulted in regaining of the enzyme acti...

Liposome-interaction induced conformation changes of glyceraldehyde-3-phosphate dehydrogenase.

Tryptophanyl emission spectra of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase (G3PDH) were measured after the addition of liposomes prepared of natural phospholipids: phosphatidylinositols (PI), phosphatidylserines (PS) and phosphatidylcholines (PC). The measurings were made for various molar lipid/protein ratios (100-1000). A decrease in the enzyme fluorescence intensity and a "red" ...

alpha-crystallin assists the renaturation of glyceraldehyde-3-phosphate dehydrogenase.

alpha-Crystallin, a major lens protein, has many of the properties of a molecular chaperone, but its ability to assist refolding of proteins has been less certain. In the present work it was shown that alpha-crystallin specifically increased the reactivation of guanidine-denatured glyceraldehyde-3-phosphate dehydrogenase with most of the activity being recovered. In the incubation mixture the r...

The isolation and specific activity of rabbit-muscle glyceraldehyde phosphate dehydrogenase.

Spectrophotometric identification of an active site-specific acyl glyceraldehyde 3-phosphate dehydrogenase. The regulation of its kinetic and equilibrium properties by coenzyme.

Glyceraldehyde 3-phosphate dehydrogenase from rabbit muscle reacts rapidly with /3-(2-furyl)acryloyl phosphate (FA-phosphate) in aqueous solutions at neutral pH to yield an active site-specific, spectrophotometrically identitlable /3-(2-furyl)acryloyl enzyme (FA-enzyme). This acyl-enzyme reacts with arsenate, phosphate, and NADH to give p-(2furyl)acrylic acid, FA-phosphate, and P-(2-furyl)acrol...