A method is reported for the preparative isolation of the two forms of pro-(carboxy-peptidase A) from pig pancreas: the monomer and the binary complex with pro-(proteinase E). This method, which is mainly based on chromatography on DEAE-Sepharose at pH 5.7, allows these proenzymes to be prepared more quickly and in safer conditions than with other reported methods. Undegraded and homogeneous carboxypeptidase A1 and A2 species (peptidyl-L-amino acid hydrolase, EC 188.8.131.52), in monomeric forms with high specific activity, are also obtained in high yield by controlled trypsin activation of either of the pro-(carboxypeptidases A) followed by chromatography on DEAE-Sepharose at pH 5.8 under dissociating conditions (7M-urea).
|Publication status||Published - 1 Jan 1985|
Vilanova, M., Vendrell, J., Lopez, T., Cuchillo, C. M., & Avilés, F. X. (1985). Preparative isolation of the two forms of pig pancreatic pro-(carboxypeptidase A) and their monomeric carboxypeptidases A. Biochemical Journal, 229(3), 605-609. https://doi.org/10.1042/bj2290605