Zn(II) complex for selective and rapid scission of protein backbone.
A ZnII complex with an aldehyde group hydrolyzed porcine pancreatic elastase under mild conditions, pH 8.0, 50 degrees C, by the Schiff base formation between the ZnII complex and the NH2 group in the protein, suggesting that a ZnII compound can be active toward peptide hydrolysis when it strongly binds to the substrate.
Yashiro
Morio
M
Department of Nanochemistry, Faculty of Engineering, Tokyo Polytechnic University, Iiyama, 1583, Atsugi, 243-0297, Japan. yashiro@nano.t-kougei.ac.jp
Kawakami
Yukiko
Y
Taya
Jun-ichi
J
Arai
Suguru
S
Fujii
Yuki
Y
D000818:Animals; D046911:Macromolecular Substances / Q000737:chemistry; D008958:Models, Molecular; D015394:Molecular Structure; D010196:Pancreatic Elastase / Q000737:chemistry*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013552:Swine; D015032:Zinc / Q000737:chemistry*
D046911:Macromolecular Substances; D010196:Pancreatic Elastase; D015032:Zinc