α-Crystallin assists the renaturation of glyceraldehyde-3-phosphate dehydrogenase

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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...

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Acetyl phosphate formation catalyzed by glyceraldehyde-3-phosphate dehydrogenase.

Glyceraldehyde-3-phosphate dehydrogenase catalyzes the oxidative phosphorylation of n-glyceraldehyde-3-phosphate to 1,3-diphosphoglyceric acid (1, 2). The enzyme also catalyzes the oxidation of n-glyceraldehyde, although the product of this reaction has not been characterized (1,2). In the present study it is shown that acetaldehyde (3), propionaldehyde, and butyraldehyde also act as substrates...

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The Mechanism of Action of Glyceraldehyde-3- Phosphate Dehydrogenase*

comprises both an oxidation and a phosphorylation and must therefore consist of two successive steps. Until recently there was considerable doubt as to which came first, the oxidation or the phosphorylation. Early speculations (l-4) that the initial step was the uptake of phosphate to form a 1,3-diphosphoglyceraldehyde have proved impossible of confirmation (5-7), and it has recently become cle...

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 2000

ISSN: 0264-6021,1470-8728

DOI: 10.1042/bj3450467