Zobrazeno 1 - 10
of 32
pro vyhledávání: '"Flora H. Pettit"'
Publikováno v:
Biochemical and Biophysical Research Communications. 179:611-614
Sulfite has been identified as an essential metabolite by means of growth studies using a chemically-defined, protein-free medium for culture of human peripheral lymphocytes. Sulfite reduced the amount of cysteine required for optimum growth by at le
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::575cf25b3cb2d111b20f7ce1606f9357
https://doi.org/10.1016/0006-291x(91)91415-9
https://doi.org/10.1016/0006-291x(91)91415-9
Publikováno v:
Drug Metabolism and Drug Interactions. 19
Hydroxymethylglutaryl-CoA reductase inhibitors (statins) are widely used to inhibit biosynthesis of cholesterol in individuals with elevated serum levels of this risk factor for cardiovascular disease. We find that statins are toxic to human lymphocy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f7e58e1d926db034e633612918bf32eb
https://doi.org/10.1515/dmdi.2003.19.3.151
https://doi.org/10.1515/dmdi.2003.19.3.151
Publikováno v:
Biochemistry. 20:4555-4560
The relationships between release of (3)H-labeled lipoyl moieties by trypsin and lipoamidase and accompanying loss of overall enzymatic activity of the Escherichia coli pyruvate and alpha-ketoglutarate dehydrogenase complexes were studied. Trypsin re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e09f8971e9ce15156616d50c89de49d1
https://doi.org/10.1021/bi00519a007
https://doi.org/10.1021/bi00519a007
Publikováno v:
Biochemical and Biophysical Research Communications. 87:244-252
Evidence is presented that dephosphorylation of the three phosphorylation sites on bovine kidney pyruvate dehydrogenase by pyruvate dehydrogenase phosphatase is random. The relative rates of dephosphorylation were in the order site 2 > site 3 > site
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::60f42309697fd68e249766b51c09df43
https://doi.org/10.1016/0006-291x(79)91672-3
https://doi.org/10.1016/0006-291x(79)91672-3
Autor:
Flora H. Pettit, Lester J. Reed, Michael H. Eley, Lynn Hamilton, Jim H. Collins, Robert M. Oliver
Publikováno v:
Proceedings of the National Academy of Sciences. 72:3068-3072
The binding of pyruvate dehydrogenase and dihydrolipoyl dehydrogenase (flavoprotein) to dihydrolipoyl transacetylase, the core enzyme of the E. coli pyruvate dehydrogenase complex [EC 1.2.4.1:pyruvate:lipoate oxidoreductase (decaryboxylating and acce
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f8e2daf36beedb60b96fc0c29c975956
https://doi.org/10.1073/pnas.72.8.3068
https://doi.org/10.1073/pnas.72.8.3068
Autor:
James R. Brown, Lester J. Reed, Gordon H. Dixon, Flora H. Pettit, David C. Watson, Stephen J. Yeaman, Eldridge T. Hutcheson, Thomas E. Roche
Publikováno v:
Biochemistry. 17:2364-2370
The highly purfied pyruvate dehydrogenase complex (EC 1.2.4.1) and uncomplexed pyruvate dehydrogenase from bovine kidney and heart mitochondria were phosphorylated and inactivated with pyruvate dehydrogenase kinase and [gamma-32P]ATP. Tryptic digesti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2373a6637f7cff14c1eafcf4730c19e1
https://doi.org/10.1021/bi00605a017
https://doi.org/10.1021/bi00605a017
Publikováno v:
Journal of Biological Chemistry. 256:514-519
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::228b7ec0a1cbb0ff8cd5390f566fe353
https://doi.org/10.1016/s0021-9258(19)70168-9
https://doi.org/10.1016/s0021-9258(19)70168-9
Publikováno v:
Biochemical and Biophysical Research Communications. 164:1348-1351
Quantitative growth responses of lymphocytes directly isolated from individual subjects in a newly developed chemically-defined, protein-free medium are used to demonstrate that supplements of both L-asparagine and a purine source, but neither alone,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f02bea76b2b0a7d9c999b9b492752dee
https://doi.org/10.1016/0006-291x(89)91817-2
https://doi.org/10.1016/0006-291x(89)91817-2
Publikováno v:
Proceedings of the National Academy of Sciences. 79:3945-3948
Endogenous kinase activity of highly purified pyruvate dehydrogenase complex from bovine kidney is markedly inhibited by N-ethylmaleimide and by certain disulfides. Inhibition by disulfides is highly specific and is reversed by thiols. 5,5'-Dithiobis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5aa735a33f00367d4fc9bae683e425ea
https://doi.org/10.1073/pnas.79.13.3945
https://doi.org/10.1073/pnas.79.13.3945
Publikováno v:
Proceedings of the National Academy of Sciences. 64:227-234
The activity of the multienzyme pyruvate dehydrogenase complexes, isolated from mitochondria of beef kidney, beef heart, and pork liver, is regulated by phosphorylation and dephosphorylation. Phosphorylation and concomitant inactivation of each of th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3d9e9c781753f738e4f85c78452b8dfd
https://doi.org/10.1073/pnas.64.1.227
https://doi.org/10.1073/pnas.64.1.227