伪结核巴氏杆菌二磷酸腺苷葡萄糖：糖原转葡萄糖基酶的纯化及性质
Purification and properties of the adenosine diphosphoglucose: glycogen transglucosylase of Pasteurella pseudotuberculosis.
作者信息
Dietzler D N, Strominger J L
出版信息
J Bacteriol. 1973 Feb;113(2):946-52. doi: 10.1128/jb.113.2.946-952.1973.
Abstract
The enzyme which catalyzes the transfer of glucosyl residues from adenosine diphospho(ADP)-glucose to glycogen has been partially purified from extracts of Pasteurella pseudotuberculosis. In contrast to other glycogen synthetases of this type, guanosine diphospho-glucose had about 5% of the activity of ADP-glucose as a glucosyl donor. Some other properties of the enzyme are described and compared to other bacterial glycogen synthetases.
摘要
已从伪结核巴氏杆菌提取物中部分纯化出一种能催化将葡糖基残基从二磷酸腺苷（ADP）-葡萄糖转移至糖原的酶。与这类其他糖原合成酶不同，二磷酸鸟苷-葡萄糖作为葡糖基供体时，其活性约为ADP-葡萄糖的5%。文中描述了该酶的其他一些特性，并与其他细菌糖原合成酶进行了比较。
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