Abstract
We recently cloned a human cDNA encoding folylpolyglutamate synthetase (FPGS) by complementation of an E. coli strain (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 in E. coli. In addition, general characteristics of the purified enzyme are discussed as well as its specificity for selected folyl and analog substrates.KeywordsDEAE CelluloseMonovalent CationAnalog SubstrateCrude Enzyme PreparationDEAE Cellulose ChromatographyThese keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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