title: Synthesis of mammalian prolylendopeptidase in Escherichia coli and analysis of the recombinant protein.
abstract: Prolylendopeptidase is a cytoplasmic serine proteinase which hydrolyses peptide bonds at the C-terminal side of prolines. Here, the expression in Escherichia coli of the cDNA coding for the enzyme from porcine brain is reported. Furthermore, the purification of active prolylendopeptidase from the extract of recombinant bacterial cells is described. The large amounts of protein obtained were used to gain insight in the substrate specificity of recombinant prolylendopeptidase, by using internally quenched fluorescent substrates.
authors.affiliation: Carlsberg Laboratory, Department of Physiology, Copenhagen-Valby, Denmark.
authors.forename: J
authors.initials: J
authors.lastname: Sommer
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D004926:Escherichia coli / Q000378:metabolism*; D008969:Molecular Sequence Data; D000085822:Prolyl Oligopeptidases; D011994:Recombinant Proteins / Q000032:analysis / Q000096:biosynthesis*; D012697:Serine Endopeptidases / Q000032:analysis / Q000096:biosynthesis*; D013379:Substrate Specificity; D013552:Swine
chemical_list: D011994:Recombinant Proteins; D012697:Serine Endopeptidases; D000085822:Prolyl Oligopeptidases