Zobrazeno 1 - 10
of 17
pro vyhledávání: '"M F, Shanahan"'
Autor:
Giles E. M. Martin, F. M. Brown, P. E. Roberts, K. B. Seamon, Peter J. F. Henderson, M. F. Shanahan
Publikováno v:
Journal of Biological Chemistry. 269:24870-24877
Forskolin is a potent inhibitor of mammalian passive glucose transporters. Here we show that forskolin is a remarkably specific inhibitor of energized D-galactose transport by the GalP sugar-H+ symport protein of Escherichia coli. Surprisingly, it do
Publikováno v:
Biochemical Journal. 272:151-158
Chemical and proteolytic digestion of intact erythrocyte glucose transporter as well as purified transporter protein has been used to localize the derivatization site for the photoaffinity agent 3-[125I]iodo-4-azido-phenethylamino-7-O-succinyldeacety
Publikováno v:
The Journal of biological chemistry. 269(40)
Forskolin is a potent inhibitor of mammalian passive glucose transporters. Here we show that forskolin is a remarkably specific inhibitor of energized D-galactose transport by the GalP sugar-H+ symport protein of Escherichia coli. Surprisingly, it do
Autor:
Jiann-Liang Lin, Kouichi Inukai, Tomoichiro Asano, Yoshitomo Oka, Hisamitsu Ishihara, Yoshio Yazaki, M. F. Shanahan, Masatoshi Kikuchi, Hideki Katagiri, Katsunori Tsukuda
GLUT1 glucose-transporter cDNA was modified to substitute leucine for Trp-388 and transfected into Chinese hamster ovary cells using the expression vector termed pMTHneo. This tryptophan residue is conserved among most of the facilitative glucose-tra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ea367e65fc51fb92c480eb3df68d568d
https://europepmc.org/articles/PMC1132448/
https://europepmc.org/articles/PMC1132448/
Publikováno v:
The Biochemical journal. 290
The tryptophan residues 388 and 412 in the glucose transporter GLUT1 were altered to leucine (L) by site-directed mutagenesis and were transiently expressed in COS-7 cells. As assessed by immunoblotting, comparable numbers of glucose transporters wer
Publikováno v:
Journal of Biological Chemistry. 262:17683-17689
An iodinated photoaffinity label for the glucose transporter, 3-iodo-4-azidophenethylamido-7-O-succinyldeacetyl-forskolin (IAPS-forskolin), has been synthesized, purified, and characterized. The I50 for inhibition of 3-O-methylglucose transport in re
Autor:
M F Shanahan
Publikováno v:
Journal of Biological Chemistry. 257:7290-7293
[3H]Cytochalasin B was found to be a natural photoaffinity ligand which at low concentrations could be photoincorporated into specific proteins of the human erythrocyte plasma membrane associated with high affinity binding sites of this molecule. In
Publikováno v:
Journal of Biological Chemistry. 260:10897-10900
A photoreactive, radioiodinated derivative of glucose, N-(4-iodoazidosalicyl)-6-amido-6-deoxyglucopyranose (IASA-glc), has been synthesized and used as a photoaffinity label for the human erythrocyte monosaccharide transporter. Photoinactivation and
Publikováno v:
The Journal of biological chemistry. 262(36)
An iodinated photoaffinity label for the glucose transporter, 3-iodo-4-azidophenethylamido-7-O-succinyldeacetyl-forskolin (IAPS-forskolin), has been synthesized, purified, and characterized. The I50 for inhibition of 3-O-methylglucose transport in re
Publikováno v:
The Journal of biological chemistry. 262(13)
Irradiation of erythrocyte ghosts in the presence of [3H]forskolin resulted in a concentration-dependent, covalent incorporation of radiolabel into several of the major membrane protein bands. Most of the incorporation occurred in four regions of the