Abstract:
:The cholecystokinin (CCK) receptor in purified plasma membranes prepared from mouse pancreatic acini had a binding affinity of 1.8 nM, an acid pH optimum between 6.0 and 6.5, and an analog specificity of CCK8 greater than CCK33 greater than desulphated CCK8 greater than CCK4. Binding of CCK to its receptor was abolished by pretreatment of plasma membranes with trypsin. When [125I]CCK was cross-linked to its receptors with disuccinimidyl suberate, and the preparation solubilized and subjected to gel electrophoresis and autoradiography, the hormone was associated with Mr 80 000 protein in both the presence and absence of the reducing agent dithiothreitol.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Sakamoto C,Williams JA,Wong KY,Goldfine IDdoi
10.1016/0014-5793(83)80343-3subject
Has Abstractpub_date
1983-01-10 00:00:00pages
63-6issue
1eissn
0014-5793issn
1873-3468journal_volume
151pub_type
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