Abstract
An iodinating enzyme was extracted from the endostyles of Molgula manhattensis and Styela clava by a combination of surfactant treatment and trypsin digestion. The solubilized enzyme was partially purified by column chromatography. The enzyme behaves as a large molecular complex (MW ∼ 340.000) and is partially hydrophobic in nature. It catalyzes the iodination of tyrosine or protein optimally at a pH of about 7.5. Iodinating activity is inhibited at concentrations of iodide above 0.5 m M. The enzyme is capable of catalyzing the coupling of iodotyrosyl residues in thyroglobulin in vitro, forming T 4 and T 3. It is suggested that the lack of significant iodothyronine formation in the endostyle in vivo is due to the absence of a suitable protein substrate rather than to an enzymatic deficiency.
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