Zobrazeno 1 - 10
of 78
pro vyhledávání: '"Randolph T. Wedding"'
Autor:
Katie Kline, Randolph T. Wedding
Publikováno v:
Physiologia Plantarum. 92:197-200
Phosphoenolpyruvate carboxylase (PEPC) from higher plants is usually assayed by using malate dehydrogenase (MDH) as a coupling enzyme. To avoid erroneous readings caused by metal ions, which convert oxaloacetate (OAA) to pyruvate, lactic dehydrogenas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c7ed44bcda47c4f541e27aaa82c7714
https://doi.org/10.1034/j.1399-3054.1994.920201.x
https://doi.org/10.1034/j.1399-3054.1994.920201.x
Publikováno v:
Plant Physiology. 104:613-616
When two different forms of phosphoenolpyruvate carboxylase (PEPC) from maize (Zea mays L.) leaves are present in an assay it is possible to estimate the ratio of Vmax to Km (V/K) for the two forms separately. This measure of the binding of the subst
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ce6a074f61fd4bc1d733b13d5417af9e
https://doi.org/10.1104/pp.104.2.613
https://doi.org/10.1104/pp.104.2.613
Autor:
Randolph T. Wedding, Min-Xian Wu
Publikováno v:
Plant and Cell Physiology. 35:569-574
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8b29c21d26d927077a4523db19681462
https://doi.org/10.1093/oxfordjournals.pcp.a078631
https://doi.org/10.1093/oxfordjournals.pcp.a078631
Autor:
Randolph T. Wedding, Min-Xian Wu
Publikováno v:
Plant Physiology. 100:382-387
Phosphoenolpyruvate carboxylase (PEPC) purified from maize (Zea mays L.) leaves associates with maize leaf chloroplast membrane in vitro. The binding of PEPC to the membrane results in enzyme inactivation. A protein isolated from a maize leaf chlorop
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f602ca5b1ea4ad2e4ae694d5d7d0a14c
https://doi.org/10.1104/pp.100.1.382
https://doi.org/10.1104/pp.100.1.382
Publikováno v:
Plant Physiology. 99:755-758
The specific activity of phosphoenolpyruvate (PEP) measured at a saturating level of substrate diminishes as the enzyme is diluted at about the same rate that specific light scattering by the diluted enzyme decreases. The presence of PEP in the assay
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d6a40d77963b0a1364fc6988d9c19cc9
https://doi.org/10.1104/pp.99.2.755
https://doi.org/10.1104/pp.99.2.755
Publikováno v:
Plant Physiology. 97:1011-1016
The chemical modification of phosphoenolpyruvate carboxylase purified from Crassula argentea leaves was studied using the fluorescence of the extrinsic probe 8-anilino-1-naphalenesulfonate. The effects of ligands on kinetic parameters of phosphoenolp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4e3f89126c4628103b8f3af0af757ce6
https://doi.org/10.1104/pp.97.3.1011
https://doi.org/10.1104/pp.97.3.1011
Publikováno v:
Archives of Biochemistry and Biophysics. 281:324-329
The molecular weights of different aggregational states of phosphoenolpyruvate carboxylase purified from the leaves of Zea mays have been determined by measurement of the molecular diameter using a Malvern dynamic light scattering spectrometer. Using
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0f5598788c31570f906539d388bd366c
https://doi.org/10.1016/0003-9861(90)90451-4
https://doi.org/10.1016/0003-9861(90)90451-4
Publikováno v:
Archives of Biochemistry and Biophysics. 278:365-372
Purified phospho enol pyruvate carboxylase from both the crassulacean acid metabolism plant Crassula argentea and the C 4 plant Zea mays was shown by kinetic studies at saturating fixed-varying concentrations of free Mg 2+ to selectively use the meta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d86f91067bf43fc9f67af116f84871d8
https://doi.org/10.1016/0003-9861(90)90272-z
https://doi.org/10.1016/0003-9861(90)90272-z
Publikováno v:
Biochemical and Biophysical Research Communications. 168:778-785
A purification procedure which yields a near homogenous preparation of phosphoenolpyruvate (PEP) car☐ylase from the leaves of Zea mays is reported. The enzyme had a final specific activity of 33.3 micromoles per minute per milligram protein. Size e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1df660e7c8d1907380035a3209864171
https://doi.org/10.1016/0006-291x(90)92389-h
https://doi.org/10.1016/0006-291x(90)92389-h
Autor:
Randolph T. Wedding, Thierry Chardot
Publikováno v:
Plant physiology. 98(2)
The effect of 5-5'-dithiobis-2-nitrobenzoate (DTNB) on the kinetic parameters and structure of phosphoenolpyruvate carboxylase purified from maize (Zea mays L.) has been studied. The V(max) is found to be independent of the presence of this thiol rea
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eee0a9a3f5e9480bf266d9359eb764df
https://pubmed.ncbi.nlm.nih.gov/16668713
https://pubmed.ncbi.nlm.nih.gov/16668713