Variants of transketolase from human erythrocytes
✍ Scribed by M.Jan Kaczmarek; Peter F. Nixon
- Book ID
- 115824446
- Publisher
- Elsevier Science
- Year
- 1983
- Tongue
- English
- Weight
- 676 KB
- Volume
- 130
- Category
- Article
- ISSN
- 0009-8981
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## Abstract Human erythrocyte transketolase (sedoheptulose‐7‐phosphate: D‐glyceraldehyde‐3‐phosphate glycolaldehyde‐transferase) was purified 8200‐fold by adsorption onto hydroxylapatite, DEAE‐cellulose treatment, acetone fractionation, and chromatography on Sephadex G‐100. The purified transketola
Human erythrocyte transketolase could be resolved from thiamin diphosphate (TDP) by acidification of the ammonium sulfate precipitate to pH 3.5, but not by other tested procedures. Resolution was 98% by chemical measurement of residual thiamin and 95% by residual enzyme activity. Reconstitution of t