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Thermal Denaturation of Native Striatal Tyrosine Hydroxylase: Increased Thermolability of the Phosphorylated Form of the Enzyme
Author(s) -
Lazar Mitchell A.,
Truscott Roger J. W.,
Raese Joachim D.,
Barchas Jack D.
Publication year - 1981
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1981.tb01641.x
Subject(s) - tyrosine hydroxylase , tyrosine 3 monooxygenase , enzyme , tyrosine , phosphorylation , striatum , biochemistry , chemistry , denaturation (fissile materials) , biology , endocrinology , dopamine , nuclear chemistry
Abstract: Tyrosine hydroxylase was purified from bovine corpus striatum. The native enzyme had a half‐life of 15 ± 3 min at 50°C. Phosphorylation of tyrosine hydroxylase with protein kinase purified from both corpus striatum and heart activated the enzyme, but activity was rapidly lost with additional preincubation of the enzyme at 30°C. Thermal denaturation studies indicated that phosphorylated tyrosine hydroxylase had a half‐life of 5 ± 2 min at 50°C.