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. 1982 Jan 1;201(1):91–94. doi: 10.1042/bj2010091

Spectral properties of the oestrogen-induced rat uterus peroxidase II and some of its derivatives.

R L Olsen, T Flatmark, C Little
PMCID: PMC1163612  PMID: 6282264

Abstract

1. The visible absorption spectrum of peroxidase II, isolated from the uterine tissue of oestradiol-treated rats, and some of its derivatives were recorded. The spectral properties of this enzyme are very similar to eosinophile peroxidase and lactoperoxidase, suggesting that these enzymes may have a similar form of haem as prosthetic group. 2. The uterine peroxidase is modified upon interaction with H2O2 and the difference spectrum of this modified enzyme is similar to that of complex II of lactoperoxidase. The modified enzyme was found to revert spontaneously to the native enzyme at rates which depended on the concentration of free enzyme and H2O2.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Anderson W. A., Kang Y. H., DeSombre E. R. Endogenous peroxidase: specific marker enzyme for tissues displaying growth dependency on estrogen. J Cell Biol. 1975 Mar;64(3):668–681. doi: 10.1083/jcb.64.3.668. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Brökelmann J., Fawcett D. W. The localization of endogenous peroxidase in the rat uterus and its induction by estradiol. Biol Reprod. 1969 Apr;1(1):59–71. doi: 10.1095/biolreprod1.1.59. [DOI] [PubMed] [Google Scholar]
  3. Chance B. The Properties of the Enzyme-Substrate Compounds of Horse-Radish and Lacto-Peroxidase. Science. 1949 Feb 25;109(2826):204–208. doi: 10.1126/science.109.2826.204-a. [DOI] [PubMed] [Google Scholar]
  4. Duffy M. J., Duffy G. Peroxidase activity as a possible marker for a functional oestradiol receptor in human breast tumours [proceedings]. Biochem Soc Trans. 1977;5(6):1738–1739. doi: 10.1042/bst0051738. [DOI] [PubMed] [Google Scholar]
  5. Hosoya T., Saito T. Comparative studies on estrogen-dependent peroxidases contained in uterine microsomes and fluid of rats and pigs. J Biochem. 1981 Jan;89(1):203–215. doi: 10.1093/oxfordjournals.jbchem.a133182. [DOI] [PubMed] [Google Scholar]
  6. Jellinck P. H., Newcombe A., Keeping H. S. Peroxidase as a marker enzyme in estrogen-responsive tissues. Adv Enzyme Regul. 1978;17:325–342. doi: 10.1016/0065-2571(79)90020-7. [DOI] [PubMed] [Google Scholar]
  7. KLEBANOFF S. J. INACTIVATION OF ESTROGEN BY RAT UTERINE PREPARATIONS. Endocrinology. 1965 Feb;76:301–311. doi: 10.1210/endo-76-2-301. [DOI] [PubMed] [Google Scholar]
  8. Keeping H. S., Jellinck P. H. Role of estrogen-induced uterine peroxidase in the metabolism of estradiol in vivo. J Steroid Biochem. 1978 Nov;9(11):1049–1054. doi: 10.1016/0022-4731(78)90030-4. [DOI] [PubMed] [Google Scholar]
  9. Klebanoff S. J., Smith D. C. Peroxidase-mediated antimicrobial activity of rat uterine fluid. Gynecol Invest. 1970;1(1):21–30. doi: 10.1159/000301903. [DOI] [PubMed] [Google Scholar]
  10. Lyttle C. R., Jellinck P. H. Metabolism of (4- 14 C)oestradiol by oestrogen-induced uterine peroxidase. Biochem J. 1972 Apr;127(3):481–487. doi: 10.1042/bj1270481. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. McNabb T., Jellinck P. H. Origin of oestrogen-induced uterine peroxidase. J Endocrinol. 1974 Aug;62(2):415–416. doi: 10.1677/joe.0.0620415. [DOI] [PubMed] [Google Scholar]
  12. Morrison M., Allen P. Z., Bright J., Jayasinghe W. Lactoperoxidase. V. Identification and isolation of lactoperoxidase from salivary gland. Arch Biochem Biophys. 1965 Jul;111(1):126–133. doi: 10.1016/0003-9861(65)90330-9. [DOI] [PubMed] [Google Scholar]
  13. Olsen R. L., Little C. The peroxidase activity of rat uterus. Eur J Biochem. 1979 Nov;101(2):333–339. doi: 10.1111/j.1432-1033.1979.tb19725.x. [DOI] [PubMed] [Google Scholar]
  14. RYTOMAA T., TEIR H. Relationship between tissue eosinophils and peroxidase activity. Nature. 1961 Oct 21;192:271–272. doi: 10.1038/192271b0. [DOI] [PubMed] [Google Scholar]
  15. Rombauts W. A., Schroeder W. A., Morrison M. Bovine lactoperoxidase. Partial characterization of the further purified protein. Biochemistry. 1967 Oct;6(10):2965–2977. doi: 10.1021/bi00862a002. [DOI] [PubMed] [Google Scholar]
  16. SCHULTZ J., SHMUKLER H. W. MYELOPEROXIDASE OF THE LEUCOCYTE OF NORMAL HUMAN BLOOD. II. ISOLATION, SPECTROPHOTOMETRY, AND AMINO ACID ANALYSIS. Biochemistry. 1964 Sep;3:1234–1238. doi: 10.1021/bi00897a009. [DOI] [PubMed] [Google Scholar]
  17. Wever R., Plat H., Hamers M. N. Human eosinophil peroxidase: a novel isolation procedure, spectral properties and chlorinating activity. FEBS Lett. 1981 Jan 26;123(2):327–331. doi: 10.1016/0014-5793(81)80320-1. [DOI] [PubMed] [Google Scholar]

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