scholarly journals Affinity Labeling of the Adenosine 5′-Monophosphate Binding Site of Rabbit Muscle Glycogen Phosphorylase b with an Adenosine 5′-Monophosphate-Cobalt(III) Complex

1973 ◽  
Vol 248 (9) ◽  
pp. 3241-3247
Author(s):  
Antoine Danchin ◽  
Henri Buc
1975 ◽  
Vol 147 (2) ◽  
pp. 369-371 ◽  
Author(s):  
G Soman ◽  
G Philip

The inhibition of rabbit muscle glycogen phosphorylase b (1,4-alpha-D-glucan--orthophosphate alpha-glucosyltransferase, EC 2.4.1.1) by aromatic compounds was examined with 15 compounds. The relative effectiveness of the inhibitors correlated well with increasing substituent constant, pi, indicating the hydrophobic nature of the binding site. The inhibition was not affected by the ionic-strength variation of the assay mixtures. The results predict that the course of chemical modification of this enzyme and the properties of the derivatives depend on the nature of the reagent and on the incorporated groups. Many of the dissimilar and sometimes contradictory results reported for chemical-modification studies and for chemically modified phosphorylase b are explained by the findings presented in the paper.


Biochemistry ◽  
1978 ◽  
Vol 17 (26) ◽  
pp. 5680-5695 ◽  
Author(s):  
Koite Titani ◽  
Atsushi Koide ◽  
Lowell H. Ericsson ◽  
Santosh Kumar ◽  
Jacques Hermann ◽  
...  

2004 ◽  
Vol 271 (11) ◽  
pp. 2280-2290 ◽  
Author(s):  
Magda N. Kosmopoulou ◽  
Demetres D. Leonidas ◽  
Evangelia D. Chrysina ◽  
Nicolas Bischler ◽  
Gerhard Eisenbrand ◽  
...  

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