Barańczyk-Kuźma A, Szymczyk T
Biochem Pharmacol. 1986 Mar 15;35(6):995-9. doi: 10.1016/0006-2952(86)90089-4.
Phenol sulfotransferase (PST) from human and bovine lung was purified about 1000-fold and the activity was measured with different acceptor substrates. Human lung PST catalyzes sulfation of both exo- and endogenous phenols, but the bovine lung enzyme only exogenous phenols. This difference in substrate specificity seems to be related to the presence of at least two different molecular forms of the enzyme: a thermostable and a thermolabile form in human lung, and two thermostable forms in bovine lung. Like the human platelet PST, the thermostable form from human lung is active with low concentrations of phenol (Km = 45 microM) and the thermolabile form with dopamine and high concentrations of phenol (Km = 909 microM). Bovine lung, which shows no catecholamine sulfating activity, contains two thermostable phenol sulfotransferases, both active with phenol but differing in their affinity to this substrate (Km = 40 microM and 335 microM, respectively).
从人肺和牛肺中纯化得到的苯酚磺基转移酶（PST）约为原来的1000倍，并使用不同的受体底物测量其活性。人肺PST催化外源性和内源性苯酚的硫酸化，但牛肺酶仅催化外源性苯酚。这种底物特异性的差异似乎与该酶至少两种不同分子形式的存在有关：人肺中有一种热稳定形式和一种热不稳定形式，牛肺中有两种热稳定形式。与人血小板PST一样，人肺中的热稳定形式在低浓度苯酚（Km = 45 microM）下具有活性，而热不稳定形式在多巴胺和高浓度苯酚（Km = 909 microM）下具有活性。牛肺没有儿茶酚胺硫酸化活性，含有两种热稳定的苯酚磺基转移酶，两者对苯酚均有活性，但对该底物的亲和力不同（分别为Km = 40 microM和335 microM）。
