乳糖生物合成酶1 .牛乳腺组织中UDPG焦磷酸化酶的纯化及性质

Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation Pub Date : 1966-10-17 DOI:10.1016/0926-6593(66)90145-7

V.S. Steelman, K.E. Ebner

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引用次数: 15

摘要

从牛乳腺丙酮粉中纯化得到了UDPG焦磷酸化酶(UTP:α-d-葡萄糖-1-磷酸尿苷基转移酶EC 2.7.7.9)。这种酶对UTP和葡萄糖- 1-磷酸具有特异性。该酶受阴离子抑制，半乳糖1-磷酸为竞争性抑制剂，Ki = 8·10−3M。这种酶需要Mg2+才能发挥活性。所有底物的Km都已测定，它们是Mg2+浓度的函数。最佳pH值在8到9之间。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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The enzymes of lactose biosynthesis I. Purification and properties of UDPG pyrophosphorylase from bovine mammary tissue

UDPG pyrophosphorylase (UTP:α-d-glucose-1-phosphate uridyltransferase EC 2.7.7.9) has been purified from bovine mammary gland acetone powder. The enzyme is specific for UTP and glucose 1-phosphate. The enzyme is inhibited by anions and galactose 1-phosphate is a competitive inhibitor, $K_{i} = 8·10^{−3} M$ . The enzyme requires Mg²⁺ for activity. The $K_{m}$ for all the substrates have been determined and they are a function of the Mg²⁺ concentration. The pH optimum is between 8 and 9.

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Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation

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