| Autor: |
Browner, M F, Nakano, K, Bang, A G, Fletterick, R J |
| Zdroj: |
Proceedings of the National Academy of Sciences of the United States of America; March 1989, Vol. 86 Issue: 5 p1443-1447, 5p |
| Abstrakt: |
The cDNA for human muscle glycogen synthase encodes a protein of 737 amino acids. The primary structure of glycogen synthase is not related either to bacterial glycogen synthase or to any glycogen phosphorylase. All nine of the serines that are phosphorylated in the rabbit muscle enzyme in vivo are conserved in the human muscle sequence. The amino- and carboxyl-terminal fragments, which contain all the phosphorylation sites, are very negatively charged. Overall the unphosphorylated protein has a charge of -13, while the fully phosphorylated inactive protein has a net charge of -31. The importance of the asymmetrical charge distribution is discussed. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
|
