Zobrazeno 1 - 10 of 22 pro vyhledávání: '"Birgit Jacobson"'
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Isolation of the Subunits of Transcarboxylase and Reconstitution of the Active Enzyme from the Subunits
Autor: Birgit Jacobson, Margaret Chuang, Fazal Ahmad, Harlanu G. Wood, William J. Brattin
Publikováno v: Journal of Biological Chemistry. 250:918-926
The separation of the 12 SH central subunit, the 5 SE peripheral metallo subunit, and the 1.3 SE biotinyl carboxyl carrier protein which are formed on the dissociation of transcarboxylase has been accomplished by molecular sieving on Bio-Gel. The 12
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::1c7291dbe18f695f63f8a1c533234adc
https://doi.org/10.1016/s0021-9258(19)41872-3
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3
THE OXIDATION OF ASCORBATE BY ELECTRON AFFINIC DRUGS AND CARCINOGENS
Autor: Marie E. Varnes, John E. Biaglow, Cameron J. Koch, Birgit Jacobson
Publikováno v: Photochemistry and Photobiology. 28:869-876
— The nitrobenzenes, the carcinogens 4-nitropyridine-N-oxide and 4-nitro-quinoline-N-oxide as well as the nitrofurans, also known to be carcinogenic, have been found to enhance the reaction of ascorbate with oxygen. The reaction results in the oxid
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bf3ff252d4c49a85bf5ae30c756e6b41
https://doi.org/10.1111/j.1751-1097.1978.tb07034.x
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4
TRANSCARBOXYLASE, VIII. ISOLATION AND PROPERTIES OF A BIOTIN-CARBOXYL CARRIER PROTEIN
Autor: Birgit Jacobson, Harland G. Wood, Brenda I. Gerwin
Publikováno v: Proceedings of the National Academy of Sciences. 64:1315-1322
Methylmalonyl CoA-oxalacetate transcarboxylase (EC 2. 1. 3. 1) from Propionibacterium shermanii is a biotin enzyme of 670,000 molecular weight containing 6 moles of biotin per mole of enzyme. The active enzyme dissociates spontaneously at low ionic s
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::e84b7e09309c65689356053a6d296517
https://doi.org/10.1073/pnas.64.4.1315
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6
Transcarboxylase
Autor: Harland G. Wood, Brenda I. Gerwin, Birgit Jacobson, Fazal Ahmad, Pierre Waegell
Publikováno v: Journal of Biological Chemistry. 245:6471-6483
Transcarboxylase (E.C.2.1.3.1), a high molecular weight biotin enzyme, dissociates in a complex fashion to inactive subunits. The rate of dissociation is increased by increasing pH and temperature and decreased by increasing concentration of protein
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::886591c91ee8614fc0d7b5b350c30ae1
https://doi.org/10.1016/s0021-9258(18)62633-x
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7
Transcarboxylase
Autor: N. G. Wrigley, N. Michael Green, Birgit Jacobson, Harland G. Wood, R. C. Valentine, Fazal Ahmad
Publikováno v: Journal of Biological Chemistry. 247:6284-6298
The molecular weights of transcarboxylase and its constituent subunits have been determined by sedimentation equilibrium and by gel electrophoresis and the organization of the subunits has been deduced from electron micrographs. The intact enzyme (mo
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::a128e58820056f604bc6af3620d2cf33
https://doi.org/10.1016/s0021-9258(19)44796-0
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10
Transcarboxylase
Autor: David G. Lygre, Harland G. Wood, Birgit Jacobson, Fazal Ahmad
Publikováno v: Journal of Biological Chemistry. 247:6299-6305
Transcarboxylase labeled with 60Co or 65Zn was isolated and purified to near homogeneity from Propionibacterium shermanii. The enzyme which is a metallo-biotin enzyme, was found to contain 7 to 8 g atoms of zinc plus cobalt per mole of transcarboxyla
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::f8d8e92a4c9ec87b3afb1e743ce25cff
https://doi.org/10.1016/s0021-9258(19)44797-2
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