Immunological analyses of the chemotactic receptor of Dictyosteleum discoideum. Identification of cDNA clones.
The cell surface cAMP receptor was excised from preparative sodium dodecyl sulfate-polyacrylamide gel electrophoresis and used to generate a polyclonal antiserum. The antiserum immunoprecipitates the two molecular weight forms of the cAMP receptor. Both forms are phosphorylated. Western blot analyses show that the antiserum is highly specific and recognizes only the two molecular weight forms of the cAMP receptor. Immunological studies indicate that both forms of the receptor are phosphorylated. Vegetative amoebae possess low levels of the cAMP receptor. Levels of the antigen increase in differentiated cells which express high cell surface cAMP binding activity. The antiserum was also used to isolate 6 lambda gt11 cDNA clones. One of those clones contains a 1.1-kilobase pair cDNA fragment which encodes for a protein of approximately 30,000-35,000 daltons. The antibody which binds to the fusion protein also recognizes the two molecular weight forms of the receptor.
D000936:Antigen-Antibody Complex; D002633:Chemotaxis; D003001:Cloning, Molecular; D004247:DNA / Q000032:analysis*; D004023:Dictyostelium / Q000235:genetics / Q000502:physiology*; D007106:Immune Sera; D011953:Receptors, Cyclic AMP / Q000032:analysis / Q000235:genetics*
D000936:Antigen-Antibody Complex; D007106:Immune Sera; D011953:Receptors, Cyclic AMP; D004247:DNA