Zobrazeno 1 - 7
of 7
pro vyhledávání: '"M.Victoria Encinas"'
Autor:
Fernando D. González-Nilo, Emilio Cardemil, M.Victoria Encinas, José Manuel Andreu, Carlos Alfonso
Publikováno v:
The International Journal of Biochemistry & Cell Biology. 34:645-656
ATP-dependent phosphoenolpyruvate (PEP) carboxykinases are found in plants and microorganisms, and catalyse the reversible formation of PEP, ADP, and CO(2) from oxaloacetate plus ATP. These enzymes vary in quaternary structure although there is signi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c1310aa4a0cfbba65e19ca1bc1f09897
https://doi.org/10.1016/s1357-2725(01)00175-3
https://doi.org/10.1016/s1357-2725(01)00175-3
Fluorescent labeling of the nucleotide site in cytosolic rat liver phosphoenolpyruvate carboxykinase
Publikováno v:
Archives of Biochemistry and Biophysics. 286:441-447
Reaction of rat liver phosphoenolpyruvate carboxykinase (GTP: oxaloacetate carboxy-lyase (transphosphorylating), EC 4.1.1.32) with the alkylating fluorescent probe N-(iodoacetylaminoethyl)-5-naphthylamine-1-sulfonic acid (1,5-I-AEDANS), results in co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6bf34afb209d393af13507be19e75de7
https://doi.org/10.1016/0003-9861(91)90063-o
https://doi.org/10.1016/0003-9861(91)90063-o
Autor:
M.Victoria Encinas, Emilio Cardemil, Laurence R. Olsen, JoséF. Díaz, JoséM. Andreu, Hughes Goldie
Publikováno v:
Biochimica et biophysica acta. 1252(1)
The secondary structure of Saccharomyces cerevisiae and Escherichia coli phospho enolpyruvate (PEP) carboxykinases was quantitatively examined using circular dichroism (CD) and Fourier transform infrared (FTIR) spectroscopies. From CD analyses, value
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fddfc0ffe3e6fae8e33772735e0b88bb
https://pubmed.ncbi.nlm.nih.gov/7548162
https://pubmed.ncbi.nlm.nih.gov/7548162
Publikováno v:
Biochimica et biophysica acta. 1164(2)
Saccharomyces cerevisiae (ATP) and cytosolic rat liver (GTP) phospho enol pyruvate carboxykinases (EC 4.1.1.49/32) have been labeled with N-(1-pyrenyl)-iodoacetamide. Reagent incorporation was completely prevented by the presence of the respective nu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8eaa043ef2c15ba6e27e391a452f7119
https://pubmed.ncbi.nlm.nih.gov/8329445
https://pubmed.ncbi.nlm.nih.gov/8329445
Publikováno v:
Biochimica et biophysica acta. 1119(1)
Saccharomyces cerevisiae phospho enol pyruvate carboxykinase (EC 4.1.1.49), inactivated by N-(iodoacetyl)-N'-(5-sulfo-1-naphthyl)ethylenediamine, incorporated 0.95 mol of the fluorescent moiety per mol of enzyme subunit. Reagent incorporation was com
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8ab7a6d44934e9d547b8fc9ae6b666af
https://pubmed.ncbi.nlm.nih.gov/1540632
https://pubmed.ncbi.nlm.nih.gov/1540632
Publikováno v:
Biochimica et biophysica acta. 1040(1)
Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase (ATP:oxaloacetate carboxy-lyase (transphosphorylating), EC 4.1.1.49) is inactivated by several thiol- and vicinal dithiol-specific reagents. Titration experiments of the enzyme with 5,5'-dith
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::db927b69dacc5fe78265a78b474ad7ea
https://pubmed.ncbi.nlm.nih.gov/2198945
https://pubmed.ncbi.nlm.nih.gov/2198945
Publikováno v:
Biochemistry. 29(19)
Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase [ATP:oxaloacetate carboxy-lyase (transphosphorylating), EC 4.1.1.49] is inactivated by the fluorescent sulfhydryl reagent N-(iodoacetyl-N'-(5-sulfo-1-naphthyl)ethylenediamine (1,5-IAEDANS). T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2f83b70f1ea38ad33eba628ec613c3b1
https://pubmed.ncbi.nlm.nih.gov/2196937
https://pubmed.ncbi.nlm.nih.gov/2196937