Purification and general properties of human folylpolyglutamate synthetase.
Purification and general properties of human folylpolyglutamate synthetase.
复制标题
人叶酰聚谷氨酸合成酶的纯化和一般性质。
DOI：
10.1007/978-1-4615-2960-6_136
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发表时间：
1993
影响因子：
--
通讯作者：
Shane,B
中科院分区：
文献类型：
--
作者：
Garrow,TA;Shane,B
We recently cloned a human cDNA encoding folylpolyglutamate synthetase (FPGS) by complementation of anE.colistrain (SF4) deficient in FPGS activity1. The open reading frame of the cDNA predicted a protein having 545 amino acids, a Mr of 60 kDa, and an estimated pI of 6.95. In this report we describe the plasmid construct used for the expression of unfused human FPGS inE.coli. In addition, general characteristics of the purified enzyme are discussed as well as its specificity for selected folyl and analog substrates.
