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首页> 外文期刊>The biochemical journal >Partial purification and characterization of chick-embryo prolyl 3-hydroxylase
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Partial purification and characterization of chick-embryo prolyl 3-hydroxylase

机译：小鸡 - 胚脯氨酰的局部纯化和表征3-羟基酶

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pProlyl 3-hydroxylase was purified up to about 5000-fold from an (NH4)2SO4 fraction of chick-embryo extract by a procedure consisting of affinity chromatography on denatured collagen linked to agarose, elution with ethylene glycol and gel filtration. The molecular weight of the purified enzyme is about 160000 by gel filtration The enzyme is probably a glycoprotein, since (a) its activity is inhibited by concanavalin A, and (b) the enzyme is bound to columns of this lectin coupled to agarose and can be eluted with a buffer containing methyl alpha-D-mannoside. The Km values for Fe2+, 2-oxoglutarate, O2 and ascorbate in the prolyl 3-hydroxylase reaction were found to be very similar to those previously reported for these co-substrates in the prolyl 4-hydroxylase and lysyl hydroxylase reactions./p
机译：通过将与与琼脂糖的变性胶原的亲和色谱组成的方法，从与琼脂糖连接的变性胶原蛋白组成的方法，纯化3-羟化酶，从（NH4）2SO4分数上纯化高达约5000倍的鸡胚提取物。纯化酶的分子量是通过凝胶过滤约160000，酶可能是糖蛋白，因为（a）其活性通过康昔洛素a抑制，并且（b）酶与琼脂糖偶联的酶结合，酶结合，酶结合酶和酶用含有甲基α-D-甘露糖苷的缓冲液洗脱。 Fe2 +，2-氧代氟醚，O 2和抗坏血酸在脯氨基3-羟化酶反应中的km值与先前报道的这些共同基质中的这些共叶酸酯和羟化物羟化酶反应的那些非常相似。

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