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Molecular Pharmacology, Vol 8, 501-510, Copyright © 1972 by the American Society for Pharmacology and Experimental Therapeutics

Production of Antibodies to Rat Liver Phenylalanine Hydroxylase Cross-reactivity with Other Pterin-Dependent Hydroxylases

PAUL A. FRIEDMAN 1, TOM LLOYD 1, and SEYMOUR KAUFMAN 1

1 Laboratory of Neurochemistry, National Institute of Mental Health, Bethesda, Maryland 20014

A potent, specific antiserum to rat liver phenylalanine hydroxylase was produced in sheep. Agar double-immunodiffusion reaction and enzyme inhibition studies revealed extensive cross-reactivity between the antiserum and phenylalanine hydroxylases from guinea pig, mouse, monkey, and human liver, as well as from rat kidney. No cross-reactivity with Pseudomonas phenylalanine hydroxylase could be demonstrated. Further studies suggested cross-reactivity with bovine adrenal and rat brain tyrosine hydroxylases, but not with rat brain tryptophan hydroxylase, rat kidney aromatic L-amino acid decarboxylase, or bovine adrenal dopamine beta-hydroxylase.

Submitted on March 31, 1972






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