scholarly journals Physicochemical and immunohistological studies of a sulfobromophthalein- and bilirubin-binding protein from rat liver plasma membranes.

1983 ◽  
Vol 71 (6) ◽  
pp. 1796-1805 ◽  
Author(s):  
W Stremmel ◽  
M A Gerber ◽  
V Glezerov ◽  
S N Thung ◽  
S Kochwa ◽  
...  
Keyword(s):  
Rat Liver ◽  
Plasma Membranes ◽  
Binding Protein ◽  
Liver Plasma Membranes ◽  
Rat Liver Plasma Membranes ◽  
Bilirubin Binding

Partial isolation and characterization of bromosulphophthalein-binding protein from rat liver plasma membranes

1982 ◽  
Vol 17 (2) ◽  
pp. 135-143 ◽  
Author(s):  
Munehiko Tanno ◽  
Hideo Yamada ◽  
Toshio Muraki ◽  
Noriaki Sekita ◽  
Makoto Shimizu ◽  
...  
Keyword(s):  
Rat Liver ◽  
Plasma Membranes ◽  
Binding Protein ◽  
Isolation And Characterization ◽  
Liver Plasma Membranes ◽  
Rat Liver Plasma Membranes ◽  
Partial Isolation

scholarly journals Lysophosphatidylcholines can modulate the activity of the glucagon-stimulated adenylate cyclase from rat liver plasma membranes

1979 ◽  
Vol 178 (1) ◽  
pp. 217-221 ◽  
Author(s):  
M D Houslay ◽  
R W Palmer
Keyword(s):  
Adenylate Cyclase ◽  
Rat Liver ◽  
Plasma Membranes ◽  
Hormone Receptors ◽  
Cyclase Activity ◽  
Adenylate Cyclase Activity ◽  
Liver Plasma Membranes ◽  
Rat Liver Plasma Membranes ◽  
Increased Sensitivity

1. Synthetic lysophosphatidylcholines inhibit the glucagon-stimulated adenylate cyclase activity of rat liver plasma membranes at concentrations two to five times lower than those needed to inhibit the fluoride-stimulated activity. 2. Specific 125I-labelled glucagon binding to hormone receptors is inhibited at concentrations similar to those inhibiting the fluoride-stimulated activity. 3. At concentrations of lysophosphatidylcholines immediately below those causing inhibition, an activation of adenylate cyclase activity or hormone binding was observed. 4 These effects are essentially reversible. 5. We conclude that the increased sensitivity of glucagon-stimulated adenylate cyclase to inhibition may be due to the lysophosphatidylcholines interfering with the physical coupling between the hormone receptor and catalytic unit of adenylate cyclase. 6. We suggest that, in vivo, it is possible that lysophosphatidylcholines may modulate the activity of adenylate cyclase only when it is in the hormone-stimulated state.

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