Analysis of the acid phosphatases of rat sensory ganglia by isoelectric focussing on polyacrylamide gels.
The acid phosphatases of rat spinal and trigeminal ganglia have been separated by isoelectric focussing on polyacrylamide gels into two main classes with pI's of 7.1 and 5.4. A low-pI acid phosphatase is also present in the mouse but not in the guinea pig. Evidence is presented that in the rat the pI 5.4 enzyme represents the nonlysosomal acid phosphatase that has been identified histochemically in one population of sensory neurones. This pI 5.4 acid phosphatase is partly membrane-bound and is selectively depleted by capsaicin administration. In lumbar dorsal root ganglia the enzyme is selectively depleted by sectioning the sciatic nerve and undergoes rapid axonal transport, a greater amount being transported peripherally than centrally. The results are discussed with reference to the possible function of this nonlysosomal acid phosphatase.
D000135:Acid Phosphatase / Q000032:analysis*; D000818:Animals; D001370:Axonal Transport; D002211:Capsaicin / Q000494:pharmacology; D005260:Female; D005724:Ganglia / Q000201:enzymology*; D005727:Ganglia, Spinal / Q000201:enzymology*; D007525:Isoelectric Focusing / Q000379:methods; D051381:Rats; D011919:Rats, Inbred Strains; D012584:Sciatic Nerve / Q000201:enzymology; D014276:Trigeminal Nerve / Q000201:enzymology
D000135:Acid Phosphatase; D002211:Capsaicin