Kojima K, Mogi M, Oka K, Nagatsu T
Neurochem Int. 1984;6(4):475-80. doi: 10.1016/0197-0186(84)90117-7.
Tyrosine hydroxylase (TH) was purified from the soluble fraction of human adrenal glands. The enzyme in human adrenal glands that was purified to apparent homogeneity had an apparent M(r) of about 280,000. Sodium dodecyl sulfate (SDS) gel electrophoresis gave a single band with a M(r) of 60,000 similar to the M(r) of bovine adrenal enzyme. The enzyme is considered to be composed of four identical subunits. The specific activity of the final preparation was approximately 310 nmol 3,4-dihydroxyphenylalanine (DOPA) formed/min/mg protein. The use of the "Western Blot" method showed that human adrenal TH did not aggregate as rapidly as bovine adrenal TH.
