The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.
Purification and characterization of the major constitutive form of testicular heme oxygenase. The noninducible isoform.
Open accessAbstract
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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
Lowry, O., Rosebrough, N., Farr, A. L., & Randall, R. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52451-6 · Cited by 317,331
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961
Towbin, H., Staehelin, T., & Gordon, J. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.9.4350 · Cited by 53,385
DISC ELECTROPHORESIS – II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS*
Davis, B. J. (1964) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1964.tb14213.x · Cited by 18,892
The enzymatic conversion of heme to bilirubin by microsomal heme oxygenase.
Tenhunen, R., Marver, H. S., & Schmid, R. (1968) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.61.2.748 · Cited by 1,803
(1962) · Postgraduate Medical Journal · doi:10.1136/pgmj.38.436.126-a · Cited by 1,457
Yasukochi, Y., & Masters, B. S. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)33166-6 · Cited by 1,178
The Golgi apparatus (complex)-(1954-1981)-from artifact to center stage.
Farquhar, M. G., & Palade, G. E. (1981) · The Journal of cell biology · doi:10.1083/jcb.91.3.77s · Cited by 996
Dulley, J. R., & Grieve, P. A. (1975) · Analytical Biochemistry · doi:10.1016/0003-2697(75)90415-7 · Cited by 947
Maines, M. D., Trakshel, G. M., & Kutty, R. K. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42488-4 · Cited by 759
Self-citation
Cited by
Heme oxygenase: Function, multiplicity, regulatory mechanisms, and clinical applications
Maines, M. D. (1988) · The FASEB Journal · doi:10.1096/fasebj.2.10.3290025 · Cited by 1,707
Self-citationSignaling to heme oxygenase-1 and its anti-inflammatory therapeutic potential
Paine, A., Eiz-Vesper, B., Blasczyk, R., & Immenschuh, S. (2010) · Biochemical Pharmacology · doi:10.1016/j.bcp.2010.07.014 · Cited by 699
Coupling Heme and Iron Metabolism via Ferritin H Chain
Gozzelino, R., & Soares, M. P. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5666 · Cited by 151
Autocatalytic radical reactions in physiological prosthetic heme modification
Colas, C., & Ortiz de Montellano, P. R. (2003) · Chemical Reviews · doi:10.1021/cr0204303 · Cited by 139
Rat liver cytochrome P-450b, P-420b, and P-420c are degraded to biliverdin by heme oxygenase
Kutty, R. K., Daniel, R. F., Ryan, D. E., Levin, W., & Maines, M. D. (1988) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(88)90492-4 · Cited by 95
Self-citation
Metadata
- Authors
- Trakshel, G. M., Kutty, R. K., & Maines, M. D.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1986-08
- Volume
- 261
- Issue
- 24
- Pages
- 11131-11137
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1538826970
- Cited by
- 259
- References
- 30
- FWCI
- 1.93
- Type
- journal article
- Language
- en
- Open access
- hybrid
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Purification and characterization of the major constitutive form of testicular heme oxygenase. The noninducible isoform. https://app.cochat.ai/papers/10.1016/s0021-9258(18)67358-2
- The paper
- Trakshel, G. M., Kutty, R. K., & Maines, M. D. (1986). Purification and characterization of the major constitutive form of testicular heme oxygenase. The noninducible isoform. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)67358-2
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
