Purification of inactive precursor of carboxypeptidase Y using selective cleavage method coupled with molecular display.
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.
Maeda
Haruko
H
Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto, Japan.
Nagayama
Mitsuru
M
Kuroda
Kouichi
K
Ueda
Mitsuyoshi
M
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
D004792:Enzyme Precursors; D043402:Cathepsin A