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Binding of Aldolase and Triosephosphate Dehydrogenase to F-Actin and Modification of Catalytic Properties of Aldolase

✍ Scribed by Heidwolf Arnold; Dirk Pette


Book ID
115112395
Publisher
John Wiley and Sons
Year
1970
Tongue
English
Weight
718 KB
Volume
15
Category
Article
ISSN
1432-1327

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πŸ“œ SIMILAR VOLUMES


Brownian dynamics of interactions betwee
✍ Stephen L. Lowe; Derek M. Atkinson; Victor F. Waingeh; Kathryn A. Thomasson πŸ“‚ Article πŸ“… 2002 πŸ› John Wiley and Sons 🌐 English βš– 387 KB

## Abstract Previous Brownian dynamics (BD) simulations (Ouporov IG, Knull HR and Thomasson KA 1999. __Biophys. J__. 76: 17–27) of complex formation between rabbit aldolase and F‐actin have identified three lysine residues (K288, K293 and K341) on aldolase and acidic residues (DEDE) at the N‐termin

Theoretical study of interactions betwee
✍ Neville Y. Forlemu; Victor F. Waingeh; Igor V. Ouporov; Stephen L. Lowe; Kathryn πŸ“‚ Article πŸ“… 2006 πŸ› Wiley (John Wiley & Sons) 🌐 English βš– 681 KB

## Abstract Interactions of the glycolytic enzyme, fructose‐1,6‐bisphosphate aldolase (aldolase), with F‐actin may be one mechanism for the colocalization of glycolytic enzymes. Examination of these interactions in different animal species tests this hypothesis by observing whether binding sites ar