Abstract
After electrophoresis impure transketolase preparations stained readily with an activity stain based on a published method, but pure preparations gave no reaction. The bands first obtained were due to the presence of (i) a transketolase- d-glyceraldehyde-3-phosphate dehydrogenase complex, (ii) alcohol dehydrogenases, and (iii) a zone of high local pH at the buffer front. Lyophilization of the reagents eliminated artifacts due to alcohol dehydrogenase. An external starch indicator gel was developed that gave colored bands with both pure and impure transketolase preparations and a similar indicator gel was developed for transaldolase.
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