Aldolase-catalysed inactivation of glyceraldehyde-3-phosphate dehydrogenase
✍ Scribed by PATTHY, LÁSZLÓ; VAS, MÁRIA
- Book ID
- 109711160
- Publisher
- Nature Publishing Group
- Year
- 1978
- Tongue
- English
- Weight
- 214 KB
- Volume
- 276
- Category
- Article
- ISSN
- 0028-0836
- DOI
- 10.1038/276094a0
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Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has long been recognized as playing an integral role in glycolysis. During the past 20 years, however, a number of novel, additional functions for GAPDH have been described. These include acting as an uracil DNA glycosylase, activator of transcription
Partially purified flounder muscle (Pseudopleuronectus americanus) glyceraldehyde 3-phosphate dehydrogenase was immobilized on cyanogen bromide-activated Sepharose. The catalytic properties of the immobilized preparation were studied to determine if immobilization alters the kinetic properties of th