Browsing by Author "Babul, A."

Now showing items 1-4 of 4

    • Characterization of Isoenzymes of Adenosine Triphosphate :D-Hexose 6-Phosphotransferase from Rat Liver 
      González González, Larry Javier; Ureta, G.; Babul, A.; Rabajille Pichara, Felipe Andrés; Niemeyer, (1967)
      Four isoenzymes of adenosine triphosphate (ATP):d-hexose 6-phosphotransferase have been separated from rat liver by DEAE-cellulose. Three of these isoenzymes (A-C) are similar to animal hexokinases inasmuch as they exhibit ...
    • Kinetic mechanism of phosphofructokinase-2 from Escherichia coli. A mutant enzyme with a different mechanism 
      Campos Campos, Maritza Pamela; Guixé Leguía, Victoria Cristina; Babul, A. (1984)
      The kinetic mechanisms of Escherichia coli phosphofructokinase-2 (Pfk-2) and of the mutant enzyme Pfk-2* were investigated. Initial velocity studies showed that both enzymes have a sequential kinetic mechanism, indicating ...
    • LoCuSS: Testing hydrostatic equilibrium in galaxy clusters 
      Smith, G. P.; Mazzotta, P.; Okabe, N.; Ziparo, F.; Mulroy, S. L.; Babul, A.; Finoguenov, A.; McCarthy, I. G.; Lieu, M.; Bahé, Y. M.; Bourdin, H.; Evrard, A. E.; Futamase, T.; Haines, Chris; Jauzac, M.; Marrone, D. P.; Martino, R.; May, P. E.; Taylor, J. E.; Umetsu, K. (Oxford University Press, 2016)
      We test the assumption of hydrostatic equilibrium in an X-ray luminosity selected sample of 50 galaxy clusters at 0.15 < z < 0.3 from the Local Cluster Substructure Survey (LoCuSS). Our weak-lensing measurements of M500 ...
    • LoCuSS: the slow quenching of star formation in cluster galaxies and the need for pre-processing 
      Haines, Chris; Pereira, M. J.; Smith, G. P.; Egami, E.; Babul, A.; Finoguenov, A.; Ziparo, F.; McGee, S. L.; Rawle, T. D.; Okabe, N.; Moran, S. M. (IOP Publishing, 2015)
      We present a study of the spatial distribution and kinematics of star-forming galaxies in 30 massive clusters at 0.15 < z < 0.30, combining wide-field Spitzer 24 mu m and GALEX near-ultraviolet imaging with highly complete ...