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 b...
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Veröffentlicht in: | Chemical communications (Cambridge, England) England), 2009-01 (12), p.1544-1546 |
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creator | Yashiro, Morio Kawakami, Yukiko Taya, Jun-ichi Arai, Suguru Fujii, Yuki |
description | 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. |
doi_str_mv | 10.1039/b818022a |
format | Article |
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subjects | Animals Macromolecular Substances - chemistry Models, Molecular Molecular Structure Pancreatic Elastase - chemistry Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Swine Zinc - chemistry |
title | Zn(II) complex for selective and rapid scission of protein backbone |
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