Further studies on tryptophan hydroxylase in rat brainstem and beef pineal

Soluble tryptophan hydroxylating enzymes have been obtained from both the beef pineal gland and rat brainstem. The enzymes have a pH optimum of 7.5 and appear to be typical aromatic ring hydroxylases. Although aniron requirement of the enzymes can be demonstrated by iron chelators, exogenous iron is...

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Veröffentlicht in:	Biochemical pharmacology 1969-05, Vol.18 (5), p.1071-1081
Hauptverfasser:	Jequier, Eric, Robinson, Donald S., Lovenberg, Walter, Sjoerdsma, Albert
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Brain Chemistry Brain Stem - enzymology Catechols - pharmacology Cattle Dihydroxyphenylalanine - pharmacology Dopamine - pharmacology Hydrogen-Ion Concentration Iron - pharmacology Iron Chelating Agents - pharmacology Methyltyrosines - pharmacology Mixed Function Oxygenases - analysis Mixed Function Oxygenases - antagonists & inhibitors Mixed Function Oxygenases - isolation & purification Norepinephrine - pharmacology Phenylalanine - analysis Phenylalanine - metabolism Pineal Gland - enzymology Pteridines - pharmacology Pyruvates - pharmacology Rats Serum Albumin - pharmacology Tryptophan - analysis Tryptophan - antagonists & inhibitors Tryptophan - isolation & purification Tryptophan - pharmacology
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