Abstract
Antibodies to tyrosine hydroxylase (TH; EC 1.14.16.2) have been extremely useful in establishing the neuronal and cellular localization of TH (Pickel et al., 1975a,b) and, recently, in demonstrating that in situ phosphorylation of TH is important in regulating the catalytic activity of TH (Waymire et al., 1979). While in the process of raising antibodies to TH, we observed an interesting property of immunoglobulins (Ig) from a sheep that was injected with TH purified from rat pheochromocytoma. Mixture of a partially purified TH and sheep Ig (0–45% ammonium sulfate) resulted in a dramatic elevation of TH activity. The following experiments were performed to establish whether this effect resulted from a specific interaction of TH and antibodies directed against TH. The results indicate that this crude Ig fraction contains anti-TH antibodies, that the majority of anti-TH activity is associated with activation of TH, and that the anti-TH antibodies are not uniformly distributed across IgG subclasses.
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Haycock, J.W., Waymire, J.C. (1981). Activating sheep antibodies to tyrosine hydroxylase. In: Usdin, E., Weiner, N., Youdim, M.B.H. (eds) Function and Regulation of Monoamine Enzymes: Basic and Clinical Aspects. Palgrave Macmillan, London. https://doi.org/10.1007/978-1-349-06276-8_13
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DOI: https://doi.org/10.1007/978-1-349-06276-8_13
Publisher Name: Palgrave Macmillan, London
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