Zobrazeno 1 - 10
of 10
pro vyhledávání: '"E H Kmiotek"'
Publikováno v:
Journal of Biological Chemistry. 263:10687-10697
Binding experiments indicate that mitochondrial aspartate aminotransferase can associate with the alpha-ketoglutarate dehydrogenase complex and that mitochondrial malate dehydrogenase can associate with this binary complex to form a ternary complex.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::65d213d93a6bbb8532af29b2f9e011a1
https://doi.org/10.1016/s0021-9258(18)38026-8
https://doi.org/10.1016/s0021-9258(18)38026-8
Publikováno v:
Journal of Biological Chemistry. 260:6069-6079
Citrate, malate, and high levels of ATP dissociate the mitochondrial aspartate aminotransferase-glutamate dehydrogenase complex and have an inhibitory effect on the latter enzyme. These effects are opposed by Mg2+, leucine, Mg2+ plus ATP, and carbamy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::321f7927b71f3820c24c2bcbb55f247c
https://doi.org/10.1016/s0021-9258(18)88939-6
https://doi.org/10.1016/s0021-9258(18)88939-6
Publikováno v:
Journal of Biological Chemistry. 263:13610-13614
Leucine and monomethyl succinate initiate insulin release, and glutamine potentiates leucine-induced insulin release. Alanine enhances and malate inhibits leucine plus glutamine-induced insulin release. The insulinotropic effect of leucine is at leas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::96f4edeebbf4737244b063c29b4a48ec
https://doi.org/10.1016/s0021-9258(18)68285-7
https://doi.org/10.1016/s0021-9258(18)68285-7
Publikováno v:
Separation Science and Technology. 14:453-474
The operating characteristics of hollow-fiber electropolarization chromato-graphy (or electrical field-flow fractionation) of proteins are surveyed. Particular attention is given to the dependence of protein retardation and electroretention on field
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a71a9b4e2d17d901b8d05c08d9e2db72
https://doi.org/10.1080/01496397908068470
https://doi.org/10.1080/01496397908068470
Publikováno v:
The Journal of biological chemistry. 263(27)
Leucine and monomethyl succinate initiate insulin release, and glutamine potentiates leucine-induced insulin release. Alanine enhances and malate inhibits leucine plus glutamine-induced insulin release. The insulinotropic effect of leucine is at leas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::e0061da79d2beedbf4254b24fd4346e4
https://pubmed.ncbi.nlm.nih.gov/3047128
https://pubmed.ncbi.nlm.nih.gov/3047128
Publikováno v:
The Journal of biological chemistry. 260(10)
Citrate, malate, and high levels of ATP dissociate the mitochondrial aspartate aminotransferase-glutamate dehydrogenase complex and have an inhibitory effect on the latter enzyme. These effects are opposed by Mg2+, leucine, Mg2+ plus ATP, and carbamy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::c47757d780a44a9e2c5c2f39a95d93f6
https://pubmed.ncbi.nlm.nih.gov/3997814
https://pubmed.ncbi.nlm.nih.gov/3997814
Publikováno v:
The Journal of biological chemistry. 263(22)
Binding experiments indicate that mitochondrial aspartate aminotransferase can associate with the alpha-ketoglutarate dehydrogenase complex and that mitochondrial malate dehydrogenase can associate with this binary complex to form a ternary complex.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::21be9a99680fced63d71f53d43859ba5
https://pubmed.ncbi.nlm.nih.gov/2899080
https://pubmed.ncbi.nlm.nih.gov/2899080
Autor:
L A, Fahien, E H, Kmiotek
Publikováno v:
Progress in clinical and biological research.
Carbamyl phosphate synthase-I can enhance glutamate dehydrogenase-mitochondrial aspartate aminotransferase interactions. These results indicate that a complex can be formed between all three enzymes, which is stable in the presence of substrates and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::c151695b36596ec79d7e56d927ec93c5
https://pubmed.ncbi.nlm.nih.gov/6718417
https://pubmed.ncbi.nlm.nih.gov/6718417
Publikováno v:
Archives of biochemistry and biophysics. 164(1)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::815945865e4ba378360a26a276eb3d48
https://pubmed.ncbi.nlm.nih.gov/4547948
https://pubmed.ncbi.nlm.nih.gov/4547948
