Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Michael A. Weibel"'
Publikováno v:
The Journal of Chemical Physics. 112:7209-7218
A molecular beam source of pure hydroxyl radicals has been developed and used to explore the water reaction catalyzed over Pt(111). An electrostatic hexapole selectively focused OD radicals from a supersonic corona discharge source onto a Pt target a
Publikováno v:
Surface Science. 444:66-78
Temperature-programmed desorption (TPD) measurements were made to probe the interactions of hydroxyl radicals (OD) with Pt(111). A pure, intense molecular beam of OD was prepared by filtering the effluent from a supersonic corona discharge D2O/He sou
Publikováno v:
The Journal of Chemical Physics. 108:3134-3141
A supersonic corona discharge source was used to produce molecular beams of plasma particles. Neutral, polar components of the plasma mixture were selectively focused by an electrostatic hexapole, thereby “simplifying” the chemical and rotational
Publikováno v:
The Journal of Physical Chemistry A. 101:7674-7683
An electrostatic hexapole was used to state-select OH and OD radicals in single, low-lying, |JΩMJ〉 rotational states. The radicals were produced in a corona discharge, supersonic molecular beam source by dissociating H2O (D2O) seeded in Ar or He.
Publikováno v:
Journal of Vacuum Science & Technology A: Vacuum, Surfaces, and Films. 15:2238-2246
Intense molecular beams of fluorocarbon radicals were generated with a corona discharge passing through a supersonic jet expansion of 15% C2F6 in Ar. An electrostatic hexapole separated the polar neutrals entrained in the beam by selectively focusing
Publikováno v:
Journal of Food Science. 39:920-926
Publikováno v:
Biotechnology and Bioengineering. 18:987-1000
An analysis of the pore diffusion model involving a two-substrate enzymatic reaction is presented. The resulting equations have been applied to the case of galactose oxidase catalyzed oxidation of galactose when the enzyme is immobilized on porous gl
Publikováno v:
Biotechnology and Bioengineering. 18:1679-1694
Galactose oxidase (E.C. 1.1.3.9) was covalently immobilized to chemically modified porous silica particles by reaction of the native enzyme with pendant benzoyl azide groups on the carrier. The enzyme loading on the carrier was 100-150 units per mill
Autor:
Michael K. Weibel, Christopher Dodge
Publikováno v:
Archives of Biochemistry and Biophysics. 169:146-151
An in vitro biochemical fuel cell based upon the enzymatically catalyzed aerobic oxidation of glucose is described. The anodic half-reaction employs an electron transfer sequence consisting of the glucose oxidase reductive half-reaction and dichloroi
Autor:
Michael K. Weibel, Harold J. Bright
Publikováno v:
Journal of Biological Chemistry. 246:2734-2744
The pH dependence of the steady state parameters of the glucose oxidase (EC 1.1.3.4, from Aspergillus niger) reaction was determined by O2-monitored experiments over the entire pH range from 3 to 10 at 25°, with d-glucose as substrate. The data were