Purification of glycogen phosphorylase from small quantities of mouse skeletal muscle

1984 ◽  
Vol 141 (2) ◽  
pp. 494-498 ◽  
Author(s):  
P.Elaine Butler ◽  
Dorothy Fairhurst ◽  
Robert J. Beynon
1985 ◽  
Vol 5 (7) ◽  
pp. 567-572 ◽  
Author(s):  
P. Elaine Butler ◽  
E. Jane Cookson ◽  
Robert J. Beynon

Pyridoxal phosphate, the cofactor of glycogen phosphorylase, fulfils the criteria needed of a turnover label for this enzyme. The decay of protein-bound label following administration of [3H]pyridoxine is a good index of the rate of degradation of the enzyme in vivo. This method has been applied to the study of catabolism of the enzyme in normal, denervated and dystrophic mouse skeletal muscle. In both of the pathological conditions the enzyme is degraded more rapidly than normal.


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Sarah J. Lessard ◽  
Amanda T. Ouchida ◽  
Hygor N. Araujo ◽  
Dawit A. Gonçalves ◽  
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Author(s):  
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Yoshifumi Tamura ◽  
Saori Kakehi ◽  
Kageumi Takeno ◽  
Minako Kawaguchi ◽  
...  

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