High affinity histamine binding site is the H3 receptor: Characterization and autoradiographic localization in rat brain

Synapse ◽  
1991 ◽  
Vol 8 (2) ◽  
pp. 144-151 ◽  
Author(s):  
Paul Cumming ◽  
Christopher Shaw ◽  
Steven R. Vincent
Life Sciences ◽  
1982 ◽  
Vol 30 (11) ◽  
pp. 953-961 ◽  
Author(s):  
J. Benavides ◽  
J.F. Rumigny ◽  
J.J. Bourguignon ◽  
C. Cash ◽  
C.G. Wermuth ◽  
...  

1980 ◽  
Vol 64 (4) ◽  
pp. 365-366 ◽  
Author(s):  
Jack E. Rosenblatt ◽  
Rebecca Del Carmen ◽  
Richard Jed Wyatt

1984 ◽  
Vol 122 (1) ◽  
pp. 265-269 ◽  
Author(s):  
R.A. Lutz ◽  
R.A. Cruciani ◽  
T. Costa ◽  
P.J. Munson ◽  
D. Rodbard

1986 ◽  
Vol 6 (1) ◽  
pp. 85-93 ◽  
Author(s):  
Pamela A Blurton ◽  
A M Broadhurst ◽  
M D Wood ◽  
M G Wyllie

1990 ◽  
Vol 267 (2) ◽  
pp. 441-445 ◽  
Author(s):  
A B Theibert ◽  
S Supattapone ◽  
C D Ferris ◽  
S K Danoff ◽  
R K Evans ◽  
...  

The two inositol phosphate-binding proteins, the Ins(1,4,5)P3 (InsP3) and Ins(1,3,4,5)P4 (InsP4) receptors, and the two particulate InsP3-metabolizing enzymes, InsP3 5-phosphatase and InsP3 3-kinase, were solubilized with detergent from rat cerebellar membranes. These four activities are shown to be distinct molecular species by separation using a variety of protein chromatographic steps. The pharmacology of the partially purified InsP4-binding site indicates that the binding has a high affinity and selectivity for InsP4 over InsP3. These results suggest the existence of a distinct specific InsP4-binding protein which may represent the receptor for this putative second messenger.


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