Immunochemical Characterization of Dopamine β‐Hydroxylase

Dopamine P-hydroxylase (EC 1.14.17.1, dopamine-P-monooxygenase; DPH) is an enzyme specific for the catecholamine-storing organelles of chromaflin cells and adrenergic neurons [25, 3 1, 36-39, 59, 96; see also Ref. 1021. The enzyme is a constituent not only of the membranes of these organelles but also of their releasable cores [ 1-5, 8, 9, 30, 50, 55-57, 58, 60, 61,63,64,69,7 1, 74, 75, 88, 971. More recent studies have shown that the two forms of DPH differ in hydrophobicity [l, 18, 60, 611 and in kinetics [l, 771, although they appear identical in overall size and in immunological properties [30, 56,63, 66, 75, 971. DPH is a notoriously unstable enzyme and is readily inactivated in vitro by a wide range of inhibitors [5, 26,40,79], which impedes quantification of the enzyme by activity measurements. However, the inactive forms do not differ from the active enzyme to such an extent that they can (d) Concluding comments The molecular properties of the bovine DBH (a) Differences between the soluble IV.

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