Homospecific activity (activity per enzyme protein) of tyrosine hydroxylase increases in parkinsonian brain.
Tyrosine hydroxylase (TH) contents in the caudate nucleus, putamen, and substantia nigra from control and parkinsonism brains were measured for the first time by a sandwich enzyme immunoassay. Both the TH protein content and TH activity (Vmax) were decreased in parallel in the parkinsonian brains as compared with those of the control brains. In contrast, TH "homospecific activity" (activity per enzyme protein) was significantly increased in the parkinsonian brains. The results indicate that the decrease of TH activity in parkinsonian brains is due to the decrease of TH protein content as a result of cell death. The increase in the "homospecific activity" of residual TH in parkinsonian brain suggests such molecular changes in TH molecules as result in a compensatory increase in TH activity.
D001923:Brain Chemistry; D002421:Caudate Nucleus / Q000201:enzymology; D003342:Corpus Striatum / Q000201:enzymology*; D006801:Humans; D007124:Immunoenzyme Techniques; D010300:Parkinson Disease / Q000201:enzymology*; D011699:Putamen / Q000201:enzymology; D013378:Substantia Nigra / Q000201:enzymology*; D014446:Tyrosine 3-Monooxygenase / Q000032:analysis / Q000378:metabolism*
D014446:Tyrosine 3-Monooxygenase