Immunocytochemical characterization of clathrin-associated proteins (CAPs). II. Immunolocalization of CAPs using selectively-absorbed IgG solutions.
Utilizing antibodies elicited by clathrin-associated proteins (CAPs) absorbed with three different antigenic states of CAPs, i.e., bound to clathrin (clathrin-CAPs complex), free in solution (CAPs) or partially cleaved by chymotrypsin (CAPs-subfragments), indicated that when CAPs are bound to clathrin an antigenic site (or sites) remain(s) unexposed and CAPs-subfragments lose antigenic sites as a result of limited proteolysis. IgG remaining in solution after absorption with CAPs-subfragments were directed against the chymotrypsin-sensitive, or accessible portions of CAPs, whereas IgG remaining after absorption with clathrin-CAPs complex were directed against the unexposed antigenic site(s) characteristic of the clathrin-CAPs complex. Immunocytochemical characterization of these selectively-absorbed IgG solutions suggests that CAPs detected during immunolocalization exist as a complex with clathrin.
D000818:Animals; D001665:Binding Sites; D002147:Calmodulin / Q000378:metabolism; D002352:Carrier Proteins / Q000276:immunology* / Q000378:metabolism; D002417:Cattle; D002966:Clathrin; D003034:Coated Pits, Cell-Membrane / Q000648:ultrastructure*; D003594:Cytoplasmic Granules / Q000648:ultrastructure; D011992:Endosomes / Q000648:ultrastructure*; D000939:Epitopes; D007074:Immunoglobulin G; D008297:Male; D008565:Membrane Proteins / Q000276:immunology* / Q000378:metabolism; D008970:Molecular Weight; D051381:Rats
D002147:Calmodulin; D002352:Carrier Proteins; D002966:Clathrin; D000939:Epitopes; D007074:Immunoglobulin G; D008565:Membrane Proteins