Differential labeling of the cell surface of single ciliary ganglion neurons in vitro.
Cationic ferritin binds in a time and concentration dependent manner to all surfaces of ciliary ganglion neurons in culture except "mounds" and "veils". In chase experiments, bound ferritin clears from the cells surfaces and forms larger and larger patches, even at low temperatures. Binding of cationic ferritin is inhibited by poly-L-lysine, potentiated by poly-L-glutamate, and not affected by neruaminidase (acylneuraminyl hydrolase, EC 3.2.1.18), hyaluronidase (hyaluronoglucosidase, hyaluronate 4-glycanhydrolase, EC 3.2.1.35), or chondroitin ABC lyase (EC 4.2.2.4).
D000643:Ammonium Chloride / Q000494:pharmacology; D000818:Animals; D001369:Axons / Q000502:physiology* / Q000648:ultrastructure; D001665:Binding Sites; D002642:Chick Embryo; D005293:Ferritins / Q000378:metabolism*; D005724:Ganglia / Q000166:cytology; D007700:Kinetics; D008239:Lysine / Q000494:pharmacology; D008854:Microscopy, Electron; D009046:Motor Neurons / Q000378:metabolism / Q000502:physiology* / Q000648:ultrastructure; D009439:Neuraminidase
D000643:Ammonium Chloride; D005293:Ferritins; D009439:Neuraminidase; D008239:Lysine