Glycogen phosphorylase activity in fat body during development of the silkworm, Bombyx mori.

1982 ◽  
Vol 46 (2) ◽  
pp. 575-576 ◽  
Author(s):  
Isao MORISHIMA ◽  
Takaichi SUIZU
Keyword(s):  
Bombyx Mori ◽  
Glycogen Phosphorylase ◽  
Fat Body ◽  
Phosphorylase Activity ◽  
Glycogen Phosphorylase Activity ◽  
Silkworm Bombyx Mori

scholarly journals Regulation of locust fat-body phosphorylase

1973 ◽  
Vol 135 (1) ◽  
pp. 37-41 ◽  
Author(s):  
S. W. Applebaum ◽  
H. M. Schlesinger
Keyword(s):  
Glycogen Phosphorylase ◽  
Fat Body ◽  
Competitive Inhibitor ◽  
Differential Centrifugation ◽  
Phosphorylase Activity ◽  
Optimum Activity ◽  
Ph Values ◽  
Glycogen Phosphorylase Activity ◽  
Glycogen Particles

1. Glycogen phosphorylase of locust fat-body was partially purified by differential centrifugation and dissociation from glycogen particles at two pH values. 2. Optimum activity was obtained at pH6.6–6.7. 3. The calculated apparent Km values for glycogen and glucose 1-phosphate were 0.08% and 10–13mm respectively. 4. 5′-AMP activated in the range 5μm–1mm. 5. Glucose 6-phosphate is a competitive inhibitor for the substrate glucose 1-phosphate (Ki=1.7mm). 5′-AMP abolishes this inhibition. Glucose weakly inhibits (Ki=25–30mm), but trehalose does not inhibit even at 100mm. 6. It is suggested that glucose 6-phosphate is a major regulator of glycogen phosphorylase activity in locust fat-body.

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