Zobrazeno 1 - 10
of 71
pro vyhledávání: '"L. P. HAGER"'
Publikováno v:
The Journal of biological chemistry. 270(18)
The low spin ferric and low and high spin ferrous forms of myoglobin, bacterial cytochrome P-450-CAM, and chloroperoxidase have been examined by Fe-K x-ray absorption edge spectroscopy. The positions of the absorption edge and the shapes of preedge a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::6f6fda216f29bc33d0c1599e302fad91
https://pubmed.ncbi.nlm.nih.gov/7737989
https://pubmed.ncbi.nlm.nih.gov/7737989
Publikováno v:
Advances in inorganic biochemistry. 10
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::668e0bba5be55ce8040680c0fe4c2db6
https://pubmed.ncbi.nlm.nih.gov/8203290
https://pubmed.ncbi.nlm.nih.gov/8203290
Autor:
Y J, Suh, L P, Hager
Publikováno v:
The Journal of biological chemistry. 266(33)
Previous studies on the chlorination reaction catalyzed by horseradish peroxidase using chlorite as the source of chlorine detected the formation of a chlorinating intermediate that was termed Compound X (Shahangian, S., and Hager, L.P. (1982) J. Bio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::7c1db5058af16c2c0a5b9d3239cae84a
https://pubmed.ncbi.nlm.nih.gov/1939231
https://pubmed.ncbi.nlm.nih.gov/1939231
Autor:
S R, Blanke, L P, Hager
Publikováno v:
The Journal of biological chemistry. 265(21)
Chloroperoxidase from Caldariomyces fumago is well documented as an extremely versatile catalyst, and studies are currently being conducted to delineate the fine structural features that allow the enzyme to possess chemical and physical similarities
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::280f4afe9d84f7a476b7ae0af2e3ea69
https://pubmed.ncbi.nlm.nih.gov/2373700
https://pubmed.ncbi.nlm.nih.gov/2373700
Publikováno v:
Journal of Biological Chemistry. 257:12878-12886
Pyruvate oxidase, a tetrameric enzyme consisting of 4 identical subunits, dissociates into apoenzyme monomers and free FAD when treated with acid ammonium sulfate in the presence of high concentrations of potassium bromide. Reconstitution of the nati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::db53426a81f0017e04ef5916500388c0
https://doi.org/10.1016/s0021-9258(18)33597-x
https://doi.org/10.1016/s0021-9258(18)33597-x
Autor:
W D Hewson, L P Hager
Publikováno v:
Journal of Biological Chemistry. 254:3182-3186
In the reaction between equimolar amounts of horseradish peroxidase and chlorite, the native enzyme is oxidized directly to Compound II (Hewson, W.D., and Hager, L.P. (1979) J. Biol. Chem. 254, 3175-3181). At acidic pH but not at alkaline values, thi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a0b8f4e384ecaa84106715c4b47c924c
https://doi.org/10.1016/s0021-9258(18)50741-9
https://doi.org/10.1016/s0021-9258(18)50741-9
Autor:
L P Hager, J A Manthey
Publikováno v:
Journal of Biological Chemistry. 256:11232-11238
A bromoperoxidase has been isolated and purified from the marine green algae, Penicillus capitatus. The purified enzyme is homogenous as determined by polyacrylamide gel electrophoresis and ultracentrifugation. Bromoperoxidase can utilize bromide ion
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3092ba36dc95a8c20cd5e2115d3cccff
https://doi.org/10.1016/s0021-9258(19)68582-0
https://doi.org/10.1016/s0021-9258(19)68582-0
Autor:
L P Hager, S Shahangian
Publikováno v:
Journal of Biological Chemistry. 257:11529-11533
Horseradish peroxidase reacts with sodium [36Clll] chlorite at pH 10.7 to form a 36Cl-labeled horseradish peroxidase intermediate. The optical absorption spectrum of this intermediate is quite stable and very similar to that of horseradish peroxidase
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fc4a6e128eac6038fe8b745ff9eae863
https://doi.org/10.1016/s0021-9258(18)33793-1
https://doi.org/10.1016/s0021-9258(18)33793-1
Autor:
L P Hager, J A Manthey
Publikováno v:
Journal of Biological Chemistry. 260:9654-9659
Bromoperoxidase Compound I has been formed in reactions between bromoperoxidase and organic peroxide substrates. The absorbance spectrum of bromoperoxidase Compound I closely resembles the Compound I spectra of other peroxidases. The pH dependence of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1a5f69f51b4bd9614f47fe87f1c5abe4
https://doi.org/10.1016/s0021-9258(17)39288-8
https://doi.org/10.1016/s0021-9258(17)39288-8
Autor:
W D Hewson, L P Hager
Publikováno v:
Journal of Biological Chemistry. 254:3175-3181
Horseradish peroxidase and chlorite, NaC102, are able to catalyze chlorination of monochlorodimedone to form dichlorodimedone. Catalytic amounts of horseradish peroxidase act to disproportionate chlorite forming chlorine dioxide and chloride ion. The
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ca4c029754f5116f1e7b5b454bd31850
https://doi.org/10.1016/s0021-9258(18)50740-7
https://doi.org/10.1016/s0021-9258(18)50740-7