Cationic colloidal gold ? a probe for light- and electron-microscopic characterization of acidic glycoconjugates using poly-l-lysine gold complex

1992 ◽  
Vol 24 (7) ◽  
pp. 419-430 ◽  
Author(s):  
Nobuyuki Kashio ◽  
Shinichiro Tsuyama ◽  
Kaori Ihida ◽  
Fusayoshi Murata
Keyword(s):  
Colloidal Gold ◽  
Gold Complex ◽  
Electron Microscopic ◽  
Cationic Colloidal Gold

scholarly journals Cytochemical characterization of sulfo- and sialoglycoconjugates of human laryngeal glandular cells.

1994 ◽  
Vol 42 (4) ◽  
pp. 485-496 ◽  
Author(s):  
M T Castells ◽  
J F Madrid ◽  
M Avilés ◽  
J A Martínez-Menárguez ◽  
J Ballesta
Keyword(s):  
Colloidal Gold ◽  
Secretory Granules ◽  
Morphological Variability ◽  
Electron Microscopic ◽  
Glandular Cells ◽  
Electron Lucent

The composition and distribution of sulfo- and sialoglycoconjugates in human laryngeal glands have been investigated at light and electron microscopic levels by use of peroxidase-, digoxigenin-, and colloidal gold-conjugated lectins in combination with several chemical and enzymatic deglycosylation procedures. The present study reveals a variety of terminal oligosaccharide sequences in serous and mucous glands. Serous cells contained glycoconjugates with terminal Neu5Ac (alpha 2-3) Gal (beta 1-4) GlcNAc, Neu5Ac (alpha 2-6) Gal/GalNAc, Neu5Ac (alpha 2-3/6) Gal (beta 1-3 GalNAc, GlcNAc, and Gal (beta 1-4) GlcNAc sequences. Scarce SO4Gal(beta 1-3)GalNAc terminal oligosaccharide chans were detected. Serous cells show wide morphological variability of secretory granules (electron lucent, electron dense, and bizonal) with different lectin affinities. Glycoconjugates in human laryngeal mucous glands contained a variety of terminal oligosaccharide sequences including SO4Gal(beta 1-4)GlcNAc, SO4Gal(beta 1-3) GalNAc, SO4GalNAc, and Neu5Ac(alpha 2-3)GalNAc.

Visualization of the anionic sites in the cell wall of apple fruit using a cationic colloidal gold probe

1993 ◽  
Vol 51 ◽  
pp. 320-321
Author(s):  
Stéphane Roy ◽  
William S. Conway ◽  
Alley E. Watada ◽  
Christopher D. Pooley ◽  
William P. Wergin
Keyword(s):  
Cell Wall ◽  
Colloidal Gold ◽  
Apple Fruit ◽  
Gold Complex ◽  
Anionic Sites ◽  
Wall Strength ◽  
Anionic Binding Sites ◽  
Cationic Colloidal Gold ◽  
Softening Process ◽  
Gold Probe

The ripening of fleshy fruits involves a softening process that consists of biochemical changes in the cell wall and leads to cell separation. Calcium is an important constituent of the cell wall and plays roles in maintaining the firmness of fruit and in reducing postharvest decay. The modification of cell wall strength is believed to be influenced by calcium that interacts with acidic pectic polymers to form crossbridges. This study examined how the frequency and distribution of anionic binding sites in the cell walls of apple fruit were influenced by calcium infiltration.Mature “Golden Delicious” apple fruits were pressure infiltrated with either H2O or a 4% solution of CaCl2 and the pericarp was sampled and processed according to standard procedures. Cationic poly-Llysine colloidal gold complex was used in a one-step procedure to visualize anionic sites in muro. Observations were performed with light microscopy, following silver intensification, and with transmission electron microscopy.

Characterization of an optimal protein A-gold complex: Improvement of the labeling efficiency

1990 ◽  
Vol 48 (3) ◽  
pp. 942-943
Author(s):  
Lucian Ghitescu ◽  
Moise Bendayan
Keyword(s):  
Polyethylene Glycol ◽  
Gold Particle ◽  
Colloidal Gold ◽  
Specific Activity ◽  
Protein A ◽  
Gold Complex ◽  
Dense Layer ◽  
Gold Particles ◽  
Optical Absorbance

By using 125I protein A, we have prepared complexes of this immunoprobe with colloidal gold particles having diameters ranging from 5 to 15 nm. Various concentrations of protein A (from 35 to 1000 nM) of known specific activity were employed in order to obtain a spectrum of conjugates differing not only in sizes, but also in amounts of protein A they carry. After ultracentrifugation through a step gradient (15, 30 and 70% w/v) of sucrose, the protein A-gold complexes were quantitatively recovered from the most dense layer, and diluted in a 0.01 M phosphate buffer containing 0.01% polyethylene glycol. The conjugates did not contain free protein A, as proven by the lack of radioactivity in the intermediate sucrose layers. By correlating the radioactivity of the complexes with their particle densities (inferred from the optical absorbance at 520 nm), the number of protein A molecules bound per gold particle was calculated for each experimental condition.

Electron Microscopic Detection and Characterization of Nonhuman Primate Enteric Viruses

1982 ◽  
Vol 40 ◽  
pp. 306-307
Author(s):  
G. C. Smith ◽  
R. L. Heberling ◽  
S. S. Kalter
Keyword(s):  
Electron Microscopy ◽  
Animal Model ◽  
Nonhuman Primate ◽  
Clinical Condition ◽  
Intestinal Tract ◽  
Enteric Viruses ◽  
Electron Microscopic ◽  
Microscopic Detection

A number of viral agents are recognized as and suspected of causing the clinical condition “gastroenteritis.” In our attempts to establish an animal model for studies of this entity, we have been examining the nonhuman primate to ascertain what viruses may be found in the intestinal tract of “normal” animals as well as animals with diarrhea. Several virus types including coronavirus, adenovirus, herpesvirus, and picornavirus (Table I) were detected in our colony; however, rotavirus, astrovirus, and calicivirus have not yet been observed. Fecal specimens were prepared for electron microscopy by procedures reported previously.

The Immuno-Electron Microscopic Localization of the Mo-Fe Protein Component of Nitrogenase in Cells of Azotobacter Vinelandii

1973 ◽  
Vol 31 ◽  
pp. 574-575
Author(s):  
J. T. Stasny ◽  
R. C. Burns ◽  
R. W. F. Hardy
Keyword(s):  
Cellular Localization ◽  
Direct Evidence ◽  
Azotobacter Vinelandii ◽  
Intracellular Localization ◽  
Protein Component ◽  
Electron Microscopic ◽  
Thin Sections ◽  
Fe Protein ◽  
Intracytoplasmic Membranes

Structure-functlon studies of biological N2-fixation have correlated the presence of the enzyme nitrogenase with increased numbers of intracytoplasmic membranes in Azotobacter. However no direct evidence has been provided for the internal cellular localization of any nitrogenase. Recent advances concerned with the crystallizatiorTand the electron microscopic characterization of the Mo-Fe protein component of Azotobacter nitrogenase, prompted the use of this purified protein to obtain antibodies (Ab) to be conjugated to electron dense markers for the intracellular localization of the protein by electron microscopy. The present study describes the use of ferritin conjugated to goat antitMo-Fe protein immunoglobulin (IgG) and the observations following its topical application to thin sections of N2-grown Azotobacter.

The Application of Protein A-Gold Immunocytochemistry to Studies of Protein Secretion

1985 ◽  
Vol 43 ◽  
pp. 426-429
Author(s):  
George H. Herbener ◽  
Antonio Nanci ◽  
Moise Bendayan
Keyword(s):  
Tissue Section ◽  
Colloidal Gold ◽  
Unit Area ◽  
Protein A ◽  
Extracellular Proteins ◽  
Gold Complex ◽  
Second Step ◽  
Igg Antibodies ◽  
Tissue Sections ◽  
Antigenic Sites

Protein A-gold immunocytochemistry is a two-step, post-embedding labeling procedure which may be applied to tissue sections to localize intra- and extracellular proteins. The key requisite for immunocytochemistry is the availability of the appropriate antibody to react in an immune response with the antigenic sites on the protein of interest. During the second step, protein A-gold complex is reacted with the antibody. This is a non- specific reaction in that protein A will combine with most IgG antibodies. The ‘label’ visualized in the electron microscope is colloidal gold. Since labeling is restricted to the surface of the tissue section and since colloidal gold is particulate, labeling density, i.e., the number of gold particles per unit area of tissue section, may be quantitated with ease and accuracy.

High-resolution transmission electron microscopic study of highly oxygen doped silicon layer

1989 ◽  
Vol 47 ◽  
pp. 692-693
Author(s):  
H. Takaoka ◽  
M. Tomita ◽  
T. Hayashi
Keyword(s):  
High Resolution ◽  
Oxygen Concentration ◽  
Silicon Layer ◽  
Detailed Structure ◽  
Electron Microscopic ◽  
Cross Sectional ◽  
Transmission Electron ◽  
Doped Silicon ◽  
Argon Ion

High resolution transmission electron microscopy (HRTEM) is the effective technique for characterization of detailed structure of semiconductor materials. Oxygen is one of the important impurities in semiconductors. Detailed structure of highly oxygen doped silicon has not clearly investigated yet. This report describes detailed structure of highly oxygen doped silicon observed by HRTEM. Both samples prepared by Molecular beam epitaxy (MBE) and ion implantation were observed to investigate effects of oxygen concentration and doping methods to the crystal structure.The observed oxygen doped samples were prepared by MBE method in oxygen environment on (111) substrates. Oxygen concentration was about 1021 atoms/cm3. Another sample was silicon of (100) orientation implanted with oxygen ions at an energy of 180 keV. Oxygen concentration of this sample was about 1020 atoms/cm3 Cross-sectional specimens of (011) orientation were prepared by argon ion thinning and were observed by TEM at an accelerating voltage of 400 kV.

Electron microscopic characterization of diamond thin films and substrates for diamond heteroepitaxial growth

1989 ◽  
Vol 47 ◽  
pp. 592-593
Author(s):  
J.B. Posthill ◽  
R.P. Burns ◽  
R.A. Rudder ◽  
Y.H. Lee ◽  
R.J. Markunas ◽  
...  
Keyword(s):  
Thin Films ◽  
Wide Band ◽  
Deposition Process ◽  
Heteroepitaxial Growth ◽  
Electron Microscopic ◽  
Wide Band Gap ◽  
Lattice Matching ◽  
Different Types ◽  
Diamond Thin Films

Because of diamond’s wide band gap, high thermal conductivity, high breakdown voltage and high radiation resistance, there is a growing interest in developing diamond-based devices for several new and demanding electronic applications. In developing this technology, there are several new challenges to be overcome. Much of our effort has been directed at developing a diamond deposition process that will permit controlled, epitaxial growth. Also, because of cost and size considerations, it is mandatory that a non-native substrate be developed for heteroepitaxial nucleation and growth of diamond thin films. To this end, we are currently investigating the use of Ni single crystals on which different types of epitaxial metals are grown by molecular beam epitaxy (MBE) for lattice matching to diamond as well as surface chemistry modification. This contribution reports briefly on our microscopic observations that are integral to these endeavors.

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