Related Experiment Video
Updated: Jun 3, 2026

Multimer-PAGE: A Method for Capturing and Resolving Protein Complexes in Biological Samples
Published on: May 5, 2017
Metal complexes as artificial proteases in proteomics: a palladium(II) complex cleaves various proteins in solutions
Frank Miskevich1, Amy Davis, Porntip Leeprapaiwong
1Department of Biological and Environmental Science, Texas A&M University at Commerce, Commerce, TX 75429, USA.
Abstract:
Most popular agents for site-specific protein cleavage are proteolytic enzymes. Because they become denatured and inactivated by detergents, enzymes are inconvenient for proteomic analysis of hydrophobic proteins which require detergents as solubilizing agents. We used cis-[Pd(en)(H(2)O)(2)](2+) (in which en represents ethylenediamine) as an artificial protease to effect cleavage of three bovine proteins, namely ubiquitin, β-casein, and serum albumin, in separate experiments. Cleavage took place in aqueous solutions containing 1.0%wt./vol. of either 3-[(3-Cholamidopropyl)dimethylammonio]-1-propanesulfonate (CHAPS) or Zwittergent 3-14 at 2.5
Related Concept Videos
Detergent Purification of Membrane Proteins
Protein-protein Interfaces
EDTA: Chemistry and Properties
Proteomics
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...
The Proteasome
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...
The Proteasome
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
