Related Experiment Video
Updated: Jul 11, 2026

Expression and Purification of Nuclease-Free Oxygen Scavenger Protocatechuate 3,4-Dioxygenase
Published on: November 8, 2019
Nucleotide sequence of cDNA for porcine heme oxygenase and its expression in Escherichia coli
1Department of Biochemistry, Yamagata University School of Medicine, Japan.
Abstract:
The nucleotide sequence of a cDNA for porcine heme oxygenase was determined. The open reading frame encoded a polypeptide of 288 amino acid residues with a molecular mass of 33,074 Da. A prokaryotic expression plasmid carrying porcine heme oxygenase cDNA was constructed and transfected into Escherichia coli cells. The full-length heme oxygenase expressed was localized in the bacterial membranes. Two small-sized heme oxygenases with no membrane-bound properties were also detected, suggesting that in E. coli cells a considerable amount of the enzyme expressed was degraded.
More Related Videos
13:16Characterization of Membrane Transporters by Heterologous Expression in E. coli and Production of Membrane Vesicles
Published on: December 31, 2019
08:01A Two-Step Strategy that Combines Epigenetic Modification and Biomechanical Cues to Generate Mammalian Pluripotent Cells
Published on: August 29, 2020
Related Concept Videos
Operons
Cell Specific Gene Expression
Protein Import into the Peroxisomes
Peroxisomal Protein Import:
Peroxisomes lack the genetic machinery required to code for their own proteins. Hence, most peroxisomal membrane, lumenal and transmembrane proteins are synthesized in the cytoplasm or ER and transported to the peroxisome...