CoChat
Sign Up
Cited by 139

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Hemin-mediated oxidative degradation of proteins.

Aft, R L, Mueller, G C·1984·Journal of Biological Chemistry
DOI 10.1016/s0021-9258(17)43657-x
Open this paper in CoChat — free account

Abstract

Hemin, in the presence of 2-mercaptoethanol and oxygen, catalyzes the selective degradation of heme-binding proteins to small peptide fragments. Among the proteins examined, the heme-binding protein of rabbit serum (HBP-93) proved to be unusually sensitive. Myoglobin also exhibited considerable sensitivity whereas hemopexin and bovine serum albumin were only slightly susceptible to this degradative action of hemin. The reaction with HBP-93 depended upon coordination of the protein with hemin, was optimal at pH 6.5 and increased 4-fold as the temperature was elevated from 10 to 60 degrees C. The requirement for both oxygen and the reducing agent, 2-mercaptoethanol, and the partial protection of HBP-93 to degradation by catalase, superoxide dismutase, mannitol, and thiourea suggest the involvement of reduced oxygen species in the reaction. A possible role for the heme-mediated degradation of proteins in cell differentiation and other biological responses is discussed.

Overview

Integrity signals

Registry

Crossref · 10.1016/s0021-9258(17)43657-x

Cites

1 of 1 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Verification

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Citations

Cites

Show all 1 references

Research works printed but not linked: 31

  1. Lo, 1981, Cancer Res., 41, 864
  2. Mager, 1979, J. Cell. Physiol., 100, 467, 10.1002/jcp.1041000310 · DOI
  3. Rutherford, 1979, Cell, 16, 415, 10.1016/0092-8674(79)90017-5 · DOI
  4. Tsutsui, 1982, Anal. Biochem., 121, 244, 10.1016/0003-2697(82)90475-4 · DOI
  5. Tsutsui, 1982, J. Biol. Chem., 257, 3925, 10.1016/S0021-9258(18)34871-3 · DOI
  6. Kumarasamy, 1979, Anal. Biochem., 95, 359, 10.1016/0003-2697(79)90739-5 · DOI
  7. Ross, 1976, Cell, 8, 513, 10.1016/0092-8674(76)90219-1 · DOI
  8. Laemmli, 1970, Nature (Lond.), 227, 680, 10.1038/227680a0 · DOI · Paper page
  9. Wray, 1981, Anal. Biochem., 118, 197, 10.1016/0003-2697(81)90179-2 · DOI
  10. Sausville, 1978, Biochemistry, 17, 2746, 10.1021/bi00607a008 · DOI
  11. Caspary, 1979, Mol. Pharmacol., 16, 256, 10.1016/S0026-895X(25)11393-X · DOI
  12. Heide, 1964, Clin. Chim. Acta, 10, 460, 10.1016/0009-8981(64)90176-7 · DOI
  13. Neuwirt, 1972, Biochim. Biophys. Acta, 264, 235, 10.1016/0304-4165(72)90287-5 · DOI
  14. Hrkal, 1974, Eur. J. Biochem., 43, 73, 10.1111/j.1432-1033.1974.tb03386.x · DOI · Paper page
  15. Muller-Eberhard, 1975, Ann. N. Y. Acad. Sci., 244, 624, 10.1111/j.1749-6632.1975.tb41558.x · DOI
  16. Muller-Eberhard, 1969, Biochem. Biophys. Res. Commun., 35, 229, 10.1016/0006-291X(69)90272-1 · DOI
  17. Myers, 1982, Biochemistry, 21, 1707, 10.1021/bi00537a001 · DOI
  18. Halliwell, 1978, FEBS Lett., 92, 321, 10.1016/0014-5793(78)80779-0 · DOI
  19. Rodriguez, 1982, Biochem. Biophys. Res. Commun., 104, 1470, 10.1016/0006-291X(82)91416-4 · DOI
  20. Suingen, 1978, Photochem. Photobiol., 28, 803, 10.1111/j.1751-1097.1978.tb07022.x · DOI
  21. Mansouri, 1973, Biochemistry, 12, 4946, 10.1021/bi00748a020 · DOI
  22. Gutteridge, 1981, FEBS Lett., 128, 343, 10.1016/0014-5793(81)80113-5 · DOI
  23. Misra, 1972, J. Biol. Chem., 247, 6960, 10.1016/S0021-9258(19)44679-6 · DOI
  24. Wallace, 1974, Biochem. Biophys. Res. Commun., 57, 1104, 10.1016/0006-291X(74)90810-9 · DOI
  25. Docherty, 1982, Biochem. Biophys. Res. Commun., 105, 1005, 10.1016/0006-291X(82)91070-1 · DOI
  26. Morgan, 1981, Biochemistry, 20, 1054, 10.1021/bi00508a002 · DOI
  27. Ishii, 1978, Nature (Lond.), 274, 373, 10.1038/274372a0 · DOI
  28. Goldberg, 1977, Annu. Rev. Biochem., 46, 823, 10.1146/annurev.bi.46.070177.004135 · DOI
  29. Craven, 1978, J. Biol. Chem., 253, 8433, 10.1016/S0021-9258(17)34310-7 · DOI
  30. Ignarro, 1982, Biochim. Biophys. Acta, 718, 49, 10.1016/0304-4165(82)90008-3 · DOI
  31. Aft, 1982, Fed. Proc., 41, 682

Cited by

Sorted by citations

Metadata

Authors
Aft, R. L., & Mueller, G. C.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1984-01
Volume
259
Issue
1
Pages
301-305
ISSN
0021-9258
DOI
10.1016/s0021-9258(17)43657-x
Cited by
139
References
1
Language
en
Licence

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