Charging and Aggregation of Positively Charged Latex Particles in the Presence of Anionic Polyelectrolytes†

2007 ◽  
Vol 111 (29) ◽  
pp. 8626-8633 ◽  
Author(s):  
Graeme Gillies ◽  
Wei Lin ◽  
Michal Borkovec
Keyword(s):  
Latex Particles ◽  
Positively Charged

Adsorption of oligonucleotides onto negatively and positively charged latex particles

1994 ◽  
Vol 83 (1) ◽  
pp. 25-31 ◽  
Author(s):  
A. Elaissari ◽  
P. Cros ◽  
C. Pichot ◽  
V. Laurent ◽  
B. Mandrand
Keyword(s):  
Latex Particles ◽  
Positively Charged

Preparation and characterization of Ag/AgO nanoshells on carboxylated polystyrene latex particles

2006 ◽  
Vol 21 (2) ◽  
pp. 349-354 ◽  
Author(s):  
Rongwei Zhang ◽  
Dan Zhang ◽  
Hui Mao ◽  
Wenlong Song ◽  
Ge Gao ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Polystyrene Latex ◽  
Infrared Transmission ◽  
X Ray Diffraction ◽  
Latex Particles ◽  
Transmission Electron ◽  
Polystyrene Latex Particles ◽  
Subsequent Decomposition ◽  
Positively Charged

Smooth and uniform Ag/AgO nanoshells (about 3–4 nm) on carboxylated polystyrene latex particles were prepared by electrostatic attraction between negatively charged –COO− on the surface of carboxylated polystyrene latex particles and positively charged Ag(NH3)2+ in the solution, and subsequent decomposition of the silver complex. The resultant nanoparticles were characterized with Fourier transform infrared, transmission electron microscopy, scanning electron microscopy, and x-ray diffraction. The effects of reducing agents, the amount of NaOH and temperature on the morphology of hybrid latex particles were discussed.

Human Fibrinogen Adsorption on Positively Charged Latex Particles

Langmuir ◽  
2014 ◽  
Vol 30 (37) ◽  
pp. 11165-11174 ◽  
Author(s):  
Paulina Żeliszewska ◽  
Anna Bratek-Skicki ◽  
Zbigniew Adamczyk ◽  
Michał Cieśla
Keyword(s):  
Human Fibrinogen ◽  
Latex Particles ◽  
Positively Charged ◽  
Fibrinogen Adsorption

Adsorption and Desorption Studies of Polyadenylic Acid onto Positively Charged Latex Particles

Langmuir ◽  
1995 ◽  
Vol 11 (4) ◽  
pp. 1261-1267 ◽  
Author(s):  
Abdelhamid Elaiessari ◽  
Christian Pichot ◽  
Thierry Delair ◽  
Philippe Cros ◽  
Robin Kuerfurst
Keyword(s):  
Adsorption And Desorption ◽  
Latex Particles ◽  
Polyadenylic Acid ◽  
Positively Charged

Protamine-DNA interaction

1978 ◽  
Vol 36 (2) ◽  
pp. 200-201
Author(s):  
D.P. Bazett-Jones ◽  
F.P. Ottensmeyer
Keyword(s):  
Small Volume ◽  
Double Helix ◽  
Dna Interaction ◽  
Dark Field ◽  
Sperm Head ◽  
Nuclear Proteins ◽  
Field Electron Microscopy ◽  
Dark Field Electron ◽  
Dna Double Helix ◽  
Positively Charged

Dark field electron microscopy has been used for the study of the structure of individual macromolecules with a resolution to at least the 5Å level. The use of this technique has been extended to the investigation of structure of interacting molecules, particularly the interaction between DNA and fish protamine, a class of basic nuclear proteins of molecular weight 4,000 daltons.Protamine, which is synthesized during spermatogenesis, binds to chromatin, displaces the somatic histones and wraps up the DNA to fit into the small volume of the sperm head. It has been proposed that protamine, existing as an extended polypeptide, winds around the minor groove of the DNA double helix, with protamine's positively-charged arginines lining up with the negatively-charged phosphates of DNA. However, viewing protamine as an extended protein is inconsistent with the results obtained in our laboratory.

A Freeze Shadow Technique for the Preparation of Soft Paint Latexes for Electron Microscopy

1977 ◽  
Vol 35 ◽  
pp. 314-315
Author(s):  
Earl R. Walter ◽  
Glen H. Bryant
Keyword(s):  
Sample Preparation ◽  
High Vacuum ◽  
Vacuum System ◽  
Latex Particles ◽  
New Methods ◽  
Diffusion Pump ◽  
Film Forming ◽  
Routine Basis ◽  
Distribution Studies ◽  
Preparation Techniques

With the development of soft, film forming latexes for use in paints and other coatings applications, it became desirable to develop new methods of sample preparation for latex particle size distribution studies with the electron microscope. Conventional latex sample preparation techniques were inadequate due to the pronounced tendency of these new soft latex particles to distort, flatten and fuse on the substrate when they dried. In order to avoid these complications and obtain electron micrographs of undistorted latex particles of soft resins, a freeze-dry, cold shadowing technique was developed. The method has now been used in our laboratory on a routine basis for several years.The cold shadowing is done in a specially constructed vacuum system, having a conventional mechanical fore pump and oil diffusion pump supplying vacuum. The system incorporates bellows type high vacuum valves to permit a prepump cycle and opening of the shadowing chamber without shutting down the oil diffusion pump. A baffeled sorption trap isolates the shadowing chamber from the pumps.

Structure and Interaction of Protamine by Dark Field Electron Microscopy

1976 ◽  
Vol 34 ◽  
pp. 160-161
Author(s):  
D.P. Bazett-Jones ◽  
F.P. Ottensmeyer
Keyword(s):  
Electron Microscopy ◽  
Dark Field ◽  
Amino Acid Sequences ◽  
Dimensional Structure ◽  
3 Dimensional ◽  
Field Electron ◽  
Proposed Model ◽  
Field Electron Microscopy ◽  
Dark Field Electron ◽  
Positively Charged

It has been shown for some time that it is possible to obtain images of small unstained proteins, with a resolution of approximately 5Å using dark field electron microscopy (1,2). Applying this technique, we have observed a uniformity in size and shape of the 2-dimensional images of pure specimens of fish protamines (salmon, herring (clupeine, Y-l) and rainbow trout (Salmo irideus)). On the basis of these images, a model for the 3-dimensional structure of the fish protamines has been proposed (2).The known amino acid sequences of fish protamines show stretches of positively charged arginines, separated by regions of neutral amino acids (3). The proposed model for protamine structure (2) consists of an irregular, right-handed helix with the segments of adjacent arginines forming the loops of the coil.

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