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Determination of Plasma Protein Adsorption on Magnetic Iron Oxides: Sample Preparation (1997)

Thode, Kai ; Lück, Martin ; Semmler, Wolfhard ; [et al.]

Springer

Pharmaceutical research 14 (1997), S. 905-910

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ISSN: 1573-904X

Keywords: iron oxides ; sample preparation ; 2-D PAGE ; plasma protein adsorption

Source: Springer Online Journal Archives 1860-2000

Topics: Chemistry and Pharmacology

Notes: Abstract Purpose. The purpose of this study was to investigate the influence of the sample preparation on the plasma protein adsorption pattern of polysaccharide-stabilized iron oxide particles by two-dimensional polyacrylamide gel electrophoresis (2-D PAGE). Methods. The iron oxide particles were incubated in vitro in human plasma for five minutes. Thereafter, four different methods for particle recovery, including adsorbed proteins from surplus plasma, were investigated: centrifugation, magnetic separation, gel filtration and membrane-based static microfiltration. Adsorbed proteins were desorbed from the particle surfaces by surfactants and analyzed by 2-D PAGE, as described elsewhere (1,2). Results. All the techniques investigated were able to separate small-size iron oxides (approx. 110 nm) and adsorbed proteins from excess plasma. The gels obtained by the different separation procedures displayed almost identical adsorption patterns. Major proteins identified were: fibrinogen, IgG, albumin and an unclassified protein of about 70 kDa with a pI value of 6.5−7.5. Conclusions. Centrifugation was regarded as the most suitable separation method due to its speed and ease of use. In contrast to gel filtration, any washing media can be used. The magnetic separation process is restricted to particles with high inducible magnetic saturation, in particular, to iron oxides with overall sizes 〉 50 nm.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1023/A:1012104017761

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Liver and spleen enhancement after intravenous injection of carboxydextran magnetite: effect of dose, delay of imaging, and field strength in anex vivo model (1996)

Caramella, Davide ; Jin, Xian-nu ; Mascalchi, Mario ; [et al.]

Springer

Magnetic resonance materials in physics, biology and medicine 4 (1996), S. 225-230

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ISSN: 1352-8661

Keywords: liver ; spleen contrast enhancement ; carboxydextran magnetite ; dose ; delayed imaging ; field strengths dependence ; ex vivo

Source: Springer Online Journal Archives 1860-2000

Topics: Medicine , Physics

Notes: Abstract It has been predicted that liver and spleen enhancement after administration of superparamagnetic contrast agents may be different, depending on the strength of the main magnetic field. With the use of anex vivo model, we investigated at 0.3, 0.5, and 1.5 T the effects on liver and spleen signal intensity of 5, 15, and 45 µmol/kg body weight of dextran magnetite (SHU 555A) in 54 rats. Nine rats served as controls. At different time delays since injection, the animals were killed, and after perfusion with saline, the liver, brain, and spleen were fixed in formalin. The specimens were embedded in an agar gel matrix and imaged with inversion recovery T1-weighted, proton density spin echo, and T2*-weighted gradient recalled echo (GRE) sequences. At each magnetic field strength, peak liver and spleen signal loss increased with increasing dose of the contrast medium. Signal loss was significantly more conspicuous after a dose of 15 than 5 µmol/kg body weight, but not after a dose of 45 compared with 15 µmol/kg. No signal change was observed in the brain. GRE images showed higher enhancement than proton density-weighted spin echo and inversion recovery images but were noisier. The enhancement showed a plateau between 30 min and 24 hours. Only the signal decrease of the liver after a low dose of contrast medium on GRE images was significantly higher (p〈0.01) at 1.5 than at 0.5 and 0.3 T. Other differences in respect to the field strength were less significant (p〈0.05) or nonsignificant. Differences in the spleen enhancement were nonsignificant. SHU 555A at a dose of 15 µmol/kg is an efficient intracellular contrast agent for liver and spleen at low, mid, and high field strength. Proton density spin echo images are probably the sequence of choice to exploit SHU 555A contrast effects and a wide time window for imaging after its intravenous injection does exist.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF01772010

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Identification of plasma proteins facilitated by enrichment on particulate surfaces: Analysis by two-dimensional electrophoresis and N-terminal microsequencing (1997)

Lück, Martin ; Schröder, Werner ; Harnisch, Stephan ; [et al.]

Weinheim : Wiley-Blackwell

Electrophoresis 18 (1997), S. 2961-2967

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ISSN: 0173-0835

Keywords: Plasma protein adsorption ; PK-120 ; Apolipoproteins ; Gelsolin ; Two-dimensional polyacrylamide gel electrophoresis ; Chemistry ; Biochemistry and Biotechnology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Chemistry and Pharmacology

Notes: Plasma protein adsorption on intravenously injectable drug carriers is regarded as an important factor for the fate of the particles in the body after their administration. Therefore, the plasma protein adsorption patterns on a number of different carrier systems were analyzed in vitro employing two-dimensional electrophoresis (2-DE). The particulate systems presented in this study were polystyrene (PS) model particles, PS nanoparticles surface-modified by adsorption of a surfactant, a commercial fat emulsion, and magnetic iron oxide particles used as contrast agents in magnetic resonance imaging. Most of the spots in the plasma protein adsorption patterns could be identified by matching the resulting 2-DE gels with a reference map of human plasma proteins. Several other proteins that indicated preferentially adsorbed proteins on the surface of the particles investigated have either not been identified on the reference map, or their identity was found to be ambiguous. The relevant proteins are all present in plasma in low abundance. Since these proteins were strongly enriched on the surface of the particles, the resulting spots on the 2-DE gels were successfully identified by N-terminal microsequencing. With this approach, two chains of spots, designated PLS:6 and PLS:8, were determined on a plasma reference map: inter-α-trypsin inhibitor family heavy chain-related protein (also named PK-120) and a dimer of fibrinogen γ, respectively. Plasma gelsolin is presented in a 2-DE adsorption pattern of PS model particles. One of the main proteins adsorbed by droplets of a commercial fat emulsion was identified as apoliprotein H. Moreover, the positions of apolipoproteins apoC-II and apoC-III were also verified on the 2-DE protein map of human plasma. Thus, protein adsorption experiments of the kind presented in this study are increasing our insight into human plasma proteins.

Additional Material: 5 Ill.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1002/elps.1150181538

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