Glucagon stimulation of adenyl-cyclase activity of cardiac muscle

1968 ◽  
Vol 55 (4) ◽  
pp. 181-182 ◽  
Author(s):  
Harry D. Brown ◽  
S. K. Chattopadhyay ◽  
W. S. Matthews
1972 ◽  
Vol 50 (12) ◽  
pp. 1673-1676 ◽  
Author(s):  
Y. A. Fontaine ◽  
C. Salmon ◽  
E. Fontaine-Bertrand ◽  
E. Burzawa-Gerard ◽  
E. M. Donaldson

The pituitary gonadotropin from a Pacific salmon (Oncorhynchus tshawytscha) stimulates adenyl cyclase activity in homogenates of ovaries from goldfish (Carassius auratus) but it is about 36 times less active than carp (Cyprinus carpio) gonadotropin. Moreover, a higher maximal stimulation of the cyclase is obtained with the more homologous (carp) gonadotropin. These results suggest the existence of a partial zoological specificity of teleost gonadotropins in their stimulating action on adenyl cyclase.


Reproduction ◽  
1974 ◽  
Vol 36 (2) ◽  
pp. 445-446
Author(s):  
C. Nugent ◽  
A Lopata ◽  
M. Gould

1972 ◽  
Vol 20 (11) ◽  
pp. 873-879 ◽  
Author(s):  
S. L. HOWELL ◽  
MARGARET WHITFIELD

A cytochemical method has been used to investigate the localization of adenyl cyclase activity in A and B cells of isolated rat islets of Langerhans. Adenosine triphosphate was initially utilized as substrate, the pyrophosphate liberated being precipitated by lead ions at its site of production. The specificity of the method was increased by the use of adenylyl-imidodiphosphate as an alternative substrate; this adenosine triphosphate analogue was not hydrolyzed by adenosine triphosphatase but provided an effective substrate for adenyl cyclase. Adenyl cyclase activity, which was found to retain its glucagon and fluoride sensitivity in glutaraldehyde-fixed tissue, was found exclusively and almost uniformly in the plasma membranes of A and B cells. Storage granule membrane, incorporated into the plasma membrane during secretion of the granule content by exocytosis, appeared to be devoid of adenyl cyclase activity.


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