Zobrazeno 1 - 10
of 12
pro vyhledávání: '"J K Teller"'
Autor:
Leonard A. Fahien, J K Teller
Publikováno v:
Journal of Biological Chemistry. 267:10411-10422
The level of aspartate aminotransferase in liver mitochondria was found to be approximately 140 microM, or 2-3 orders of magnitude higher than its dissociation constant in complexes with the inner mitochondrial membrane and the high molecular weight
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5a8fd3d28b2cd1a1b900f4f180af675e
https://doi.org/10.1016/s0021-9258(19)50035-7
https://doi.org/10.1016/s0021-9258(19)50035-7
Publikováno v:
Journal of Biological Chemistry. 267:10423-10432
Kinetic studies of Morris 7777 hepatoma mitochondrial NAD(P) malic enzyme were consistent with an ordered mechanism where NAD adds to the enzyme before malate and dissociation of NADH from the enzyme is rate-limiting. In addition to its active site,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::49eb865621c84d3a231430924ed16891
https://doi.org/10.1016/s0021-9258(19)50036-9
https://doi.org/10.1016/s0021-9258(19)50036-9
Publikováno v:
Journal of Biological Chemistry. 265:19486-19494
The inner mitochondrial membranes from bovine heart, rat liver, and Morris hepatoma 7777 all bound the mitochondrial isozymes of aspartate aminotransferase and malate dehydrogenase with comparable affinities and binding ratios (mg of enzyme bound per
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::773105041a376b2f4a25c0c581f66676
https://doi.org/10.1016/s0021-9258(17)45399-3
https://doi.org/10.1016/s0021-9258(17)45399-3
Publikováno v:
Neurobiology of disease. 8(1)
The carboxy-terminal fragments (CTFs) of the amyloid precursor protein (APP) are considered beta-amyloid (Abeta) precursors as well as molecular species possibly amyloidogenic and neurotoxic by [corrected] in vitro or in animal models. The CTF's role
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::aa6c8eeb18a08f8219aa32c12fb41a93
https://pubmed.ncbi.nlm.nih.gov/11162251
https://pubmed.ncbi.nlm.nih.gov/11162251
Autor:
L A, Fahien, J K, Teller
Publikováno v:
The Journal of biological chemistry. 267(15)
The level of aspartate aminotransferase in liver mitochondria was found to be approximately 140 microM, or 2-3 orders of magnitude higher than its dissociation constant in complexes with the inner mitochondrial membrane and the high molecular weight
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::7756297bd7c448192b95348b20b202a0
https://pubmed.ncbi.nlm.nih.gov/1350279
https://pubmed.ncbi.nlm.nih.gov/1350279
Publikováno v:
The Journal of biological chemistry. 267(15)
Kinetic studies of Morris 7777 hepatoma mitochondrial NAD(P) malic enzyme were consistent with an ordered mechanism where NAD adds to the enzyme before malate and dissociation of NADH from the enzyme is rate-limiting. In addition to its active site,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a1702fa31289bc31873a4c0cbfc7a6ef
https://pubmed.ncbi.nlm.nih.gov/1587826
https://pubmed.ncbi.nlm.nih.gov/1587826
Publikováno v:
The Journal of biological chemistry. 265(32)
The inner mitochondrial membranes from bovine heart, rat liver, and Morris hepatoma 7777 all bound the mitochondrial isozymes of aspartate aminotransferase and malate dehydrogenase with comparable affinities and binding ratios (mg of enzyme bound per
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::886263fffd3697dd1573d29113b9f957
https://pubmed.ncbi.nlm.nih.gov/2246239
https://pubmed.ncbi.nlm.nih.gov/2246239
Publikováno v:
Molecular pharmacology. 37(6)
In the presence of Mg2+, pure glutamate dehydrogenase is more reactive with NADPH than with NADH and is markedly activated by elevations in the ADP/ATP ratio or the addition of leucine. Because these are properties of glutamate dehydrogenase in mitoc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::6c37ee30e424dc0fa3d98feef121470e
https://pubmed.ncbi.nlm.nih.gov/2359406
https://pubmed.ncbi.nlm.nih.gov/2359406
Autor:
J. K. Teller
Publikováno v:
Archives Internationales de Physiologie et de Biochimie. 95:433-437
The effect of nucleotides: AMP, cAMP, ADP, ATP, GDP and GTP, on glutamate dehydrogenase (GDH) purified from the mealworm fat body was studied. Guanine nucleotides and ATP inhibited the enzyme strongly in both directions. GDH was partially protected f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0ce6da6f23a121cad6b1c77fe922c745
https://doi.org/10.3109/13813458709113153
https://doi.org/10.3109/13813458709113153
Publikováno v:
Journal of Biological Chemistry. 264:12303-12312
We have found previously (Fahien, L.A., Kmiotek, E.H., MacDonald, M. J., Fibich, B., and Mandic, M. (1988) J. Biol. Chem. 263, 10687-10697) that glutamate-malate oxidation can be enhanced by cooperative binding of mitochondrial aspartate aminotransfe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::af457a32c0ec8d000cd0bc0775d7b3c6
https://doi.org/10.1016/s0021-9258(18)63859-1
https://doi.org/10.1016/s0021-9258(18)63859-1