Results 191 to 200 of about 34,103 (213)
Some of the next articles are maybe not open access.

Nucleoredoxin regulates glucose metabolism via phosphofructokinase 1

Biochemical and Biophysical Research Communications, 2013
Phosphofructokinase (PFK) 1 is a glycolytic enzyme, and its abnormality contributes to the development of multiple human diseases, such as cancer. Here, we report that nucleoredoxin (NRX), a thioredoxin-related oxidoreductase, is a novel interacting partner of PFK1. NRX binds directly to PFK1, and endogenous NRX and PFK1 interact in vivo.
Yosuke, Funato   +4 more
openaire   +2 more sources

Properties of 1-phosphofructokinase from Pseudomonas piutida

Canadian Journal of Microbiology, 1977
The 1-phosphofructokinase (1-PFK, EC 2.7.1.56) from Pseudomonas putida was partially purified by a combination of (NH4)2SO4 fractionation and DEAE-Sephadex column chromatography. In its kinetic properties, this enzyme resembled the 1-PFK's from other bacteria.
S S, Bang, P, Baumann, M H, Sawyer
openaire   +2 more sources

Properties of phosphofructokinase 1 fromPythium ultimum andAgaricus bisporus and comparison with other fungal phosphofructokinases 1

Experimental Mycology, 1991
Abstract Phosphofructokinase 1 was partially purified from Agaricus bisporus fruit bodies and Pythium ultimum mycelium. The enzyme from A. bisporus was similar to other fungal phosphofructokinases 1: it was inhibited by ATP, had sigmoidal kinetics toward fructose-6-phosphate, and was stimulated by fructose-2,6-bisphosphate. Phosphoenolpyruvate was
Andre´J. Van Laere, Hilde M. Joosen
openaire   +1 more source

Characterization of 1-phosphofructokinase from halophilic archaebacterium Haloarcula vallismortis

Biochimica et Biophysica Acta (BBA) - General Subjects, 1994
1-Phosphofructokinase (EC 2.7.1.56) (1PFK) was purified and characterized for the first time from an archaebacterial halophile Haloarcula vallismortis. The purification procedure involving (NH4)2SO4 fractionation, (NH4)2SO4-mediated chromatography on Sepharose 4B, CM-cellulose chromatography, hydrophobic chromatography on phenyl Sepharose and ...
V, Rangaswamy, W, Altekar
openaire   +2 more sources

KINETIC MODEL OF PHOSPHOFRUCTOKINASE-1 FROMESCHERICHIA COLI

Journal of Bioinformatics and Computational Biology, 2008
This paper presents a kinetic model of phosphofructokinase-1 from Escherichia coli. A complete catalytic cycle has been reconstructed based on available information on the oligomeric structure of the enzyme and kinetic mechanism of its monomer. Applying the generalization of the Monod–Wyman–Changeux approach proposed by Popova and Sel'kov35–37to the ...
Kirill, Peskov   +2 more
openaire   +2 more sources

Escherichia coli phosphofructokinase: Inhibition by 8-anilino-1-naphthalenesulfonate

Archives of Biochemistry and Biophysics, 1975
Abstract Phosphofructokinase was purified 1200-fold from extracts of Escherichia coli B. Kinetic studies of the enzyme were carried out in the presence of the fluorescent dye 8-anilino-1-naphthalenesulfonate (1,8-ANS). 1,8-ANS was competitive with ATP and an uncompetitive inhibitor with respect to fructose-6- P .
S H, Liu, C M, Phillippe, C C, Griffin
openaire   +2 more sources

Home - About - Disclaimer - Privacy