dc.creator | Niemeyer, Hermann | |
dc.creator | Cerpa, Carlos | |
dc.creator | Rabajille, Eliana | |
dc.date.accessioned | 2018-12-20T14:08:22Z | |
dc.date.available | 2018-12-20T14:08:22Z | |
dc.date.created | 2018-12-20T14:08:22Z | |
dc.date.issued | 1987 | |
dc.identifier | Archives of Biochemistry and Biophysics, Volumen 257, Issue 1, 2018, Pages 17-26 | |
dc.identifier | 10960384 | |
dc.identifier | 00039861 | |
dc.identifier | 10.1016/0003-9861(87)90538-8 | |
dc.identifier | https://repositorio.uchile.cl/handle/2250/154199 | |
dc.description.abstract | Mammalian and yeast hexokinases were found to be reversibly inhibited by fructose 2,6-bisphosphate, an effect requiring the presence of a cytosolic protein factor. Experimental evidence suggests that this factor (inhibitor) is a regulatory protein, the interactions of which with hexokinases are modulated by fructose 2,6-bisphosphate. The Vmax of hexokinase D was decreased, and no changes on other kinetic parameters were observed. The inhibitor was present in fresh liver cytosol filtered through Sephadex G-25 and was partially isolated by negative absorption on DEAE-cellulose followed by ammonium sulfate fractionation. The inhibitor was also present in brain and kidney, but not in muscle. A molecular mass of 200,000 was determined by gel filtration. The inhibition was dependent on the concentrations of both the inhibitory protein and fructose 2,6-bisphosphate. No delay in fructose 2,6-bisphosphate inhibition was observed. Several other hexose phosphates were tested and were not effectiv | |
dc.language | en | |
dc.rights | http://creativecommons.org/licenses/by-nc-nd/3.0/cl/ | |
dc.rights | Attribution-NonCommercial-NoDerivs 3.0 Chile | |
dc.source | Archives of Biochemistry and Biophysics | |
dc.subject | Biophysics | |
dc.subject | Biochemistry | |
dc.subject | Molecular Biology | |
dc.title | Inhibition of hexokinase activity by a fructose 2,6-Bisphosphate-dependent cytosolic protein from liver | |
dc.type | Artículo de revista | |