Literature summary for 1.14.14.18 extracted from

Ishikawa, K.; Takeuchi, N.; Takahashi, S.; Matera, K.M.; Sato, M.; Shibahara, S.; Rousseau, D.L.; Ikeda-Saito, M.; Yoshida, T.
Heme oxygenase-2. Properties of the heme complex of the purified tryptic fragment of recombinant human heme oxygenase-2 (1995), J. Biol. Chem., 270, 6345-6350.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression of heme oxygenase-2 in Escherichia coli	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	recombinant heme oxygenase-2 expressed in Escherichia coli	Homo sapiens	16020	-

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
36000	-	x * 36000, recombinant heme oxygenase-2, SDS-PAGE	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
ammonium sulfate, Sephadex G-75, DEAE-cellulose, hydroxyapatite, tryptic 28000 Da fragment of recombinant heme oxygenase-2	Homo sapiens

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
0.017	-	28000 Da recombinant tryptic fragment of heme oxygenase-2	Homo sapiens

Subunits

Subunits	Comment	Organism
?	x * 36000, recombinant heme oxygenase-2, SDS-PAGE	Homo sapiens

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Release 2023.1 (January 2023)