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- W1969733833 abstract "The cDNA for PSP 94 , a cysteine-rich protein secreted by the human prostate, was unidirectionally digested with exonuclease III to generate deletion mutants with varying 5' ends. These were placed under the control of the lac promoter of the Bluescribe plasmid (pbs) to encode hybrid proteins containing the N terminus of β-galactosidase (βGal) and various fragments of PSP 94 . Escherichia coli clones transformed by these constructs and expressing PSP 94 epitopes were identified by radioimmunoassay of cellular and periplasmic extracts. One such clone (I-25) secreted most of its immunoreactive material into the periplasmic space. Nucleotide sequencing showed that a new consensus ribosome-binding site had been generated fortuitously, allowing expression of pre-PSP 94 free of any βSGal sequence. Periplasmic PSP 94 is indistinguishable from the natural human protein, indicating correct processing and folding of this cysteine-rich protein in bacteria." @default.
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- W1969733833 date "1988-12-01" @default.
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- W1969733833 title "Correct processing and secretion of a human prostatic secretory protein (PSP94) in Escherichia coli" @default.
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- W1969733833 doi "https://doi.org/10.1016/0378-1119(88)90512-4" @default.
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