DARPP-32 like protein in specific snail (Helix aspersa) neurones.
Monoclonal antibodies to DARPP-32 recognise an antigen which is present in specific neurones in the snail (Helix aspersa). Consecutive sections 10-microns-thick processed for the localisation of DARPP-32 and tyrosine-hydroxylase immunoreactivity did not show a coexistence in any neuronal structures. DARPP-32 positive cells were, however, often morphologically closely associated with tyrosine-hydroxylase positive cells, implying a functional relationship consistent with the proposed role of DARPP-32. Immunochemical analysis of the DARPP-32 immunoreactive material in the snail nervous system shows that the substance has a molecular weight of 28 kDa and therefore different from the DARPP-32 protein found in the rat brain.
Nuffield Laboratory of Ophthalmology, University of Oxford, UK.
N N
NN
Osborne
N L
NL
Barnett
N J
NJ
Morris
D000818:Animals; D000911:Antibodies, Monoclonal; D015153:Blotting, Western; D001923:Brain Chemistry; D051937:Dopamine and cAMP-Regulated Phosphoprotein 32; D006372:Helix, Snails / Q000032:analysis*; D007150:Immunohistochemistry; D009419:Nerve Tissue Proteins / Q000032:analysis*; D009474:Neurons / Q000737:chemistry* / Q000201:enzymology; D010750:Phosphoproteins / Q000032:analysis*; D051381:Rats; D015398:Signal Transduction; D014446:Tyrosine 3-Monooxygenase / Q000032:analysis
D000911:Antibodies, Monoclonal; D051937:Dopamine and cAMP-Regulated Phosphoprotein 32; D009419:Nerve Tissue Proteins; D010750:Phosphoproteins; D014446:Tyrosine 3-Monooxygenase