The practice of quantitative gel electrophoresis (Advanced methods in the biological sciences

1986 ◽  
Vol 5 (6) ◽  
pp. XXIV
Author(s):  
Z. Deyl
Keyword(s):  
Biological Sciences ◽  
Gel Electrophoresis

scholarly journals An alternative way to stain the gel in gel electrophoresis without causing contamination

2022 ◽  
Author(s):  
Charlotte Siu ◽  
Ashley Hitchler ◽  
Xiao Wen Cheng
Keyword(s):  
Biological Sciences ◽  
Dna Sequence ◽  
Gel Electrophoresis ◽  
Forensic Investigations

Gel electrophoresis is an important invention that can help us separate molecules based on size and charge. It has been used in many circumstances, including analysing the DNA sequence during forensic investigations and obviously, in many disciplines regarding microbiology and biological sciences as a whole. The biggest headache that comes with gel electrophoresis is the part that requires staining of a gel. Very often, if not well done, it will cause contamination and splash. In this poster, we talked about a different way to stain the gel used in gel electrophoresis without causing too much contamination

Ultrastructural localization of specific nucleoprotein fractions

1978 ◽  
Vol 36 (2) ◽  
pp. 204-205
Author(s):  
G. L. Brown
Keyword(s):  
Gel Electrophoresis ◽  
Mouse Liver ◽  
Polyacrylamide Gel Electrophoresis ◽  
Ultrastructural Localization ◽  
Polyacrylamide Gel ◽  
Acid Extraction ◽  
Acid Solutions ◽  
Low Salt ◽  
Liver Nuclei ◽  
Phosphate Groups

Bismuth (Bi) stains nucleoproteins (NPs) by interacting with available amino and primary phosphate groups. These two staining mechanisms are distinguishable by glutaraldehyde crosslinking (Fig. 1,2).Isolated mouse liver nuclei, extracted with salt and acid solutions, fixed in either formaldehyde (form.) or gl utaraldehyde (glut.) and stained with Bi, were viewed to determine the effect of the extractions on Bi stainina. Solubilized NPs were analyzed by SDS-polyacrylamide gel electrophoresis.Extraction with 0.14 M salt does not change the Bi staining characteristics (Fig. 3). 0.34 M salt reduces nucleolar (Nu) staining but has no effect on interchromatinic (IC) staining (Fig. 4). Proteins responsible for Nu and glut.- insensitive IC staining are removed when nuclei are extracted with 0.6 M salt (Fig. 5, 6). Low salt and acid extraction prevents Bi-Nu staining but has no effect on IC staining (Fig. 7). When nuclei are extracted with 0.6 M salt followed by low salt and acid, all Bi-staining components are removed (Fig. 8).

Molecular Structure of the Outermost Cell Wall Component of Spirillum Serpens

1977 ◽  
Vol 35 ◽  
pp. 342-343
Author(s):  
Wah Chiu ◽  
David Grano
Keyword(s):  
Molecular Structure ◽  
Cell Wall ◽  
Outer Membrane ◽  
Gel Electrophoresis ◽  
Electron Microscopic Examination ◽  
Electron Microscopic ◽  
Cell Wall Component ◽  
Protein Components ◽  
Exposure Technique ◽  
Structural Aspects

The periodic structure external to the outer membrane of Spirillum serpens VHA has been isolated by similar procedures to those used by Buckmire and Murray (1). From SDS gel electrophoresis, we have found that the isolated fragments contain several protein components, and that the crystalline structure is composed of a glycoprotein component with a molecular weight of ∽ 140,000 daltons (2). Under an electron microscopic examination, we have visualized the hexagonally-packed glycoprotein subunits, as well as the bilayer profile of the outer membrane. In this paper, we will discuss some structural aspects of the crystalline glycoproteins, based on computer-reconstructed images of the external cell wall fragments.The specimens were prepared for electron microscopy in two ways: negatively stained with 1% PTA, and maintained in a frozen-hydrated state (3). The micrographs were taken with a JEM-100B electron microscope with a field emission gun. The minimum exposure technique was essential for imaging the frozen- hydrated specimens.

Dynamical Scattering in Crystalline Biological Specimens. I. Criteria of Validity for Scattering Approximations

1975 ◽  
Vol 33 ◽  
pp. 192-193
Author(s):  
Robert M. Glaeser ◽  
Bing K. Jap
Keyword(s):  
Biological Sciences ◽  
Electron Microscopy ◽  
Electron Microscope ◽  
Electron Diffraction ◽  
Born Approximation ◽  
Materials Science ◽  
Image Data ◽  
Dynamical Effect ◽  
Crystallographic Structure ◽  
Electron Microscope Image

The dynamical scattering effect, which can be described as the failure of the first Born approximation, is perhaps the most important factor that has prevented the widespread use of electron diffraction intensities for crystallographic structure determination. It would seem to be quite certain that dynamical effects will also interfere with structure analysis based upon electron microscope image data, whenever the dynamical effect seriously perturbs the diffracted wave. While it is normally taken for granted that the dynamical effect must be taken into consideration in materials science applications of electron microscopy, very little attention has been given to this problem in the biological sciences.

The Application of Ultra-Thin Sectioning Techniques to Non-Biological Samples

1968 ◽  
Vol 26 ◽  
pp. 332-333
Author(s):  
C. F. Oster
Keyword(s):  
Biological Sciences ◽  
Epoxy Resin ◽  
Cross Sections ◽  
Biological Samples ◽  
Industrial Applications ◽  
Photographic Film ◽  
Silver Particles ◽  
Thin Sectioning ◽  
Embedding Medium

Although ultra-thin sectioning techniques are widely used in the biological sciences, their applications are somewhat less popular but very useful in industrial applications. This presentation will review several specific applications where ultra-thin sectioning techniques have proven invaluable.The preparation of samples for sectioning usually involves embedding in an epoxy resin. Araldite 6005 Resin and Hardener are mixed so that the hardness of the embedding medium matches that of the sample to reduce any distortion of the sample during the sectioning process. No dehydration series are needed to prepare our usual samples for embedding, but some types require hardening and staining steps. The embedded samples are sectioned with either a prototype of a Porter-Blum Microtome or an LKB Ultrotome III. Both instruments are equipped with diamond knives.In the study of photographic film, the distribution of the developed silver particles through the layer is important to the image tone and/or scattering power. Also, the morphology of the developed silver is an important factor, and cross sections will show this structure.

Interrelationship of the cellular distribution and secretion of regular structure (RS) protein in Bacillus licheniformis nm 105

1992 ◽  
Vol 50 (1) ◽  
pp. 712-713
Author(s):  
Xiaorong Zhu ◽  
Richard McVeigh ◽  
Bijan K. Ghosh
Keyword(s):  
Alkaline Phosphatase ◽  
Bacillus Licheniformis ◽  
Self Assembly ◽  
Gel Electrophoresis ◽  
Culture Supernatant ◽  
Regular Structure ◽  
The Self ◽  
Cellular Distribution ◽  
Structural Protein ◽  
Laboratory Cultures

A mutant of Bacillus licheniformis 749/C, NM 105 exhibits some notable properties, e.g., arrest of alkaline phosphatase secretion and overexpression and hypersecretion of RS protein. Although RS is known to be widely distributed in many microbes, it is rarely found, with a few exceptions, in laboratory cultures of microorganisms. RS protein is a structural protein and has the unusual properties to form aggregate. This characteristic may have been responsible for the self assembly of RS into regular tetragonal structures. Another uncommon characteristic of RS is that enhanced synthesis and secretion which occurs when the cells cease to grow. Assembled RS protein with a tetragonal structure is not seen inside cells at any stage of cell growth including cells in the stationary phase of growth. Gel electrophoresis of the culture supernatant shows a very large amount of RS protein in the stationary culture of the B. licheniformis. It seems, Therefore, that the RS protein is cotranslationally secreted and self assembled on the envelope surface.

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