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Updated: Aug 5, 2026
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Orthogonal Protein Purification Facilitated by a Small Bispecific Affinity Tag
Published on: January 16, 2012
Purification and characterization of protein Z from rabbit liver cytosol
Biochemical and Biophysical Research Communications
|October 30, 1985
Abstract:
Protein Z was purified from rabbit liver cytosol by affinity chromatography on oleic acid-agarose and preparative sodium dodecyl sulfate-polyacrylamide gel electrophoresis. After removal of sodium dodecyl sulfate, the renatured protein was found to bind heme and bilirubin with a Kd of approximately 1 microM which produced large red shifts in their absorption spectra. On isoelectric focusing, rabbit protein Z exhibited two main bands with pI around 6.0.
