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J. Biol. Chem., Vol. 261, Issue 24, 11131-11137, 08, 1986
GM Trakshel, RK Kutty and MD Maines
Recently we reported on the presence of two isoforms of heme oxygenase in
rat liver microsomes, referred to as HO-1 and HO-2, and that only HO- 1 is
inducible (Maines, M. D., Trakshel, G. M., and Kutty, R. K. (1986) J. Biol.
Chem. 261, 411-419). Presently we report on the detection of two isoforms
of the enzyme in rat testis and purification to near homogeneity of the
noninducible isoform, HO-2. A comparative characterization of the liver
HO-1 and the testicular HO-2 is also provided. The relative abundance of
the isoforms in the two organs was dissimilar. In the testis, the
predominant form was HO-2, and only minute amounts of HO-1 were detected.
In the liver, however, a 1:2 ratio of HO-1 to HO-2 was noted. The activity
of HO-2 in both organs was refractory to cadmium, an inducer of the hepatic
HO-1. Under nondenaturing electrophoresis conditions, HO-2 showed a higher
mobility than HO-1; on a sodium dodecyl sulfate-polyacrylamide gel, HO-2
displayed a higher monomeric Mr. The apparent Mr values for HO-2 and HO- 1
were 36,000 and 30,000, respectively. The isoforms differed in
immunochemical properties. Antiserum to the liver HO-1 did not recognize
the testicular HO-2 when examined by double immunodiffusion or by Western
immunoblotting. HO-2 was more sensitive to heat inactivation than HO-1.
When exposed at 65 degrees C (10 min), 70% of HO-1 activity was retained;
however, nearly 80% of HO-2 activity was lost. The apparent Km values for
heme for HO-1 and HO-2 were 0.24 and 0.40 microM, respectively. HO-1 and
HO-2 had similar requirements for cofactor and flavoprotein reductase and
were inhibited by heme-ligands (CO, KCN, NaN3). HO-2 utilized as substrate,
Fe-protoporphyrin, Fe- hematoporphyrin, and Fe-hematoporphyrin acetate; it
did not degrade intact purified rat liver cytochromes b5 and P-450 LM2,
catalase, cytochrome c, hemoglobin, or myoglobin.
Purification and characterization of the major constitutive form of testicular heme oxygenase. The noninducible isoform
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