A Novel and Simple Approach to Element Fractionation Analysis: Single Step Fractionation of Milk

2022 ◽  
pp. 132162
Author(s):  
Feyzullah Tokay ◽  
Sema Bağdat
2021 ◽  
Author(s):  
Mohammad Mehdi Moarefdoust ◽  
Shohreh Jahani ◽  
Mehran Moradalizadeh ◽  
Mohammad Mehdi Motaghi ◽  
Mohammad Mehdi Foroughi

The current study was designed to develop a single-step and simple approach to effectively fabricate three-dimensional raspberry-like In3+/NiO hierarchical nanostructure (In3+/NiO RLHNSs) as a modifier, which was subsequently characterized by...


Author(s):  
E. A. Kenik ◽  
J. Bentley

Cliff and Lorimer (1) have proposed a simple approach to thin foil x-ray analy sis based on the ratio of x-ray peak intensities. However, there are several experimental pitfalls which must be recognized in obtaining the desired x-ray intensities. Undesirable x-ray induced fluorescence of the specimen can result from various mechanisms and leads to x-ray intensities not characteristic of electron excitation and further results in incorrect intensity ratios.In measuring the x-ray intensity ratio for NiAl as a function of foil thickness, Zaluzec and Fraser (2) found the ratio was not constant for thicknesses where absorption could be neglected. They demonstrated that this effect originated from x-ray induced fluorescence by blocking the beam with lead foil. The primary x-rays arise in the illumination system and result in varying intensity ratios and a finite x-ray spectrum even when the specimen is not intercepting the electron beam, an ‘in-hole’ spectrum. We have developed a second technique for detecting x-ray induced fluorescence based on the magnitude of the ‘in-hole’ spectrum with different filament emission currents and condenser apertures.


2005 ◽  
Vol 173 (4S) ◽  
pp. 240-240
Author(s):  
Premal J. Desai ◽  
David A. Hadley ◽  
Lincoln J. Maynes ◽  
D. Duane Baldwin

2004 ◽  
Vol 49 (4) ◽  
pp. 401-403
Author(s):  
Richard B. Makover

1996 ◽  
Vol 75 (03) ◽  
pp. 497-502 ◽  
Author(s):  
Hadewijch L M Pekelharing ◽  
Henne A Kleinveld ◽  
Pieter F C.C.M Duif ◽  
Bonno N Bouma ◽  
Herman J M van Rijn

SummaryLp(a) is an LDL-like lipoprotein plus an additional apolipoprotein apo(a). Based on the structural homology of apo(a) with plasminogen, it is hypothesized that Lp(a) interferes with fibrinolysis. Extracellular matrix (ECM) produced by human umbilical vein endothelial cells was used to study the effect of Lp(a) and LDL on plasminogen binding and activation. Both lipoproteins were isolated from the same plasma in a single step. Plasminogen bound to ECM via its lysine binding sites. Lp(a) as well as LDL were capable of competing with plasminogen binding. The degree of inhibition was dependent on the lipoprotein donor as well as the ECM donor. When Lp(a) and LDL obtained from one donor were compared, Lp(a) was always a much more potent competitor. The effect of both lipoproteins on plasminogen binding was reflected in their effect on plasminogen activation. It is speculated that Lp(a) interacts with ECM via its LDL-like lipoprotein moiety as well as via its apo(a) moiety.


Sign in / Sign up

Export Citation Format

Share Document