Subcellular localization of human glyceraldehyde-3-phosphate dehydrogenase is independent of its glycolytic function
β Scribed by Jennifer L. Mazzola; Michael A. Sirover
- Book ID
- 117481222
- Publisher
- Elsevier Science
- Year
- 2003
- Tongue
- English
- Weight
- 342 KB
- Volume
- 1622
- Category
- Article
- ISSN
- 0304-4165
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## Abstract Recent studies establish that the glycolytic protein, glyceraldehydeβ3βphosphate dehydrogenase (GAPDH), is not simply a classical metabolic protein involved in energy production. Instead, it is a multifunctional protein with defined functions in numerous subcellular processes. New inves
## Abstract The elucidation of the subcellular localization of enzymes by the classical technique of homogenization followed by differential centrifugation is limited in that it is difficult to determine the effect of the severe disruptive procedures on the normal relationship of the enzymes to the
The glycolytic protein glyceraldehyde-3-phosphate dehydrogenase (GAPDH) appeared to be an archtypical protein of limited excitement. However, independent studies from a number of different laboratories reported a variety of diverse biological properties of the GAPDH protein. As a membrane protein, G