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- W2012472316 abstract "We used the prokaryotic expression vector, ptrpL1, for the expression in Escherichia coli K-12 of a cDNA clone specific for the human lysosomal hydrolase, α-galactosidase A. The 5' terminus of the cDNA clone was engineered so that an ATG codon precedes the first codon of the mature form of the enzyme. A clone with elevated expression of this human enzyme was constructed by increasing the distance between the Shine-Dalgarno site and the ATG start codon from 6 to 8 bp. Clones with α-galactosidase A specific cDNA encoding the proenzyme produce a protein of 45 kDa, the size expected for the intact proenzyme. The 45-kDa protein is specifically precipitated by antibody to α-galactosidase A, and its expression is repressed by tryptophan and induced by 3-β-indoleacrylic acid as expected for this expression vector. The human enzyme is produced in E. coli in a catalytically active form at levels sufficient to support the growth of cells using α-galactosides as sole sources of carbon and energy. In addition, bacterial colonies that produce the human enzyme turn blue in the presence of 5-bromo-4-chloro-3-indolyl-α-D-galactopyranoside." @default.
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- W2012472316 date "1987-01-01" @default.
- W2012472316 modified "2023-10-17" @default.
- W2012472316 title "Expression of the human α-galactosidase A in Escherichia coli K-12" @default.
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- W2012472316 doi "https://doi.org/10.1016/0378-1119(87)90119-3" @default.
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