title: Purification of inactive precursor of carboxypeptidase Y using selective cleavage method coupled with molecular display.
abstract: A novel purification system for inactive precursor proteins without conventional time-consuming purification steps was established. We purified an inactive precursor protein, procarboxypeptidase Y (proCPY), which was displayed on the cell surface of yeast, due to difficulty of purifying it by a system in which it is produced in cells.
authors.affiliation: Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto, Japan.
authors.forename: Haruko
authors.initials: H
authors.lastname: Maeda
authors.forename: Mitsuru
authors.initials: M
authors.lastname: Nagayama
authors.forename: Kouichi
authors.initials: K
authors.lastname: Kuroda
authors.forename: Mitsuyoshi
authors.initials: M
authors.lastname: Ueda
mesh_terms: D043402:Cathepsin A / Q000302:isolation & purification* / Q000378:metabolism; D004792:Enzyme Precursors / Q000302:isolation & purification* / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000166:cytology / Q000201:enzymology*; D013379:Substrate Specificity
chemical_list: D004792:Enzyme Precursors; D043402:Cathepsin A