@article {10.3844/ajbbsp.2005.103.106,
article_type = {journal},
title = {Use of Cross-linking to Assess Subunit Interaction of Recombinant Human Coproporphyrinogen Oxidase},
author = {Stephenson, Jason R. and Thomas, Nancy E. and Friesen, Jon A. and Jones, Marjorie A.},
volume = {1},
number = {2},
year = {2005},
month = {Jun},
pages = {103-106},
doi = {10.3844/ajbbsp.2005.103.106},
url = {https://thescipub.com/abstract/ajbbsp.2005.103.106},
abstract = {To provide further evidence for a dimeric form of coproporphyrinogen oxidase reported using the conventional hydrodynamic methods, bifunctional cross-linkers were incubated with purified, recombinant human coproporphyrinogen oxidase to determine subunit interaction in solution. The use of cross-linkers provides an effective way to demonstrate subunit association and allows for assessment of activity upon covalent cross-linking. Following incubation with selected cross-linkers, enzyme apparent molecular weight was evaluated using SDS-PAGE and enzymatic activity was monitored by spectroscopy following HPLC. The predominate multimeric form of coproporphyrinogen oxidase observed had a mass that corresponded to a dimer, indicating that coproporphyrinogen oxidase most likely functions as a homodimer in solution.},
journal = {American Journal of Biochemistry and Biotechnology},
publisher = {Science Publications}
}