scholarly journals Measurement of Globular Protein Molecules by Electron Microscopy

1960 ◽  
Vol 7 (4) ◽  
pp. 613-618 ◽  
Author(s):  
Cecil E. Hall
Keyword(s):  
Electron Microscopy ◽  
Alcohol Dehydrogenase ◽  
Molecular Species ◽  
Spherical Shape ◽  
Virus Protein ◽  
Molecular Weights ◽  
Liver Alcohol Dehydrogenase ◽  
Deposited Metal ◽  
Glutamic Dehydrogenase ◽  
Organic Particles

A series of molecular species with approximately spherical shape and with molecular weights between 35,000 and 250,000 were shadowed with platinum while resting on a cleaved mica surface. They were backed, stripped from the surface, and examined by electron microscopy. Materials examined were: pepsin, liver alcohol dehydrogenase, yeast alcohol dehydrogenase, glutamic dehydrogenase, polyhedral virus protein (insect), fibrinogen substructure, alkaline phosphatase, and microsomal particles from Escherichia coli. Measurements were made of widths perpendicular to the shadowing direction and heights were deduced from shadow lengths. For those molecular species with well established molecular weights the average heights correlate very well with the diameter of the theoretical sphere but the average widths are too great by 50 to 80 A due to the lateral growth of the deposited metal. Although the distortion in shape of shadowed particles is relatively large, with standardized conditions for shadowing, it is possible to make allowance for the distortion and to obtain reasonably reliable estimates of the dimensions of spherical organic particles down to a molecular weight of about 35,000.

DSC Study of Biocompatible Magnetite Nanoparticles Coated with Polymer

2014 ◽  
Vol 782 ◽  
pp. 611-614
Author(s):  
Alena Juríková ◽  
Kornel Csach ◽  
Jozef Miškuf ◽  
Martina Koneracká ◽  
Vlasta Závišová ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Magnetite Nanoparticles ◽  
Magnetic Particles ◽  
Weight Ratio ◽  
Spherical Shape ◽  
Biocompatible Polymers ◽  
Hydrophilic Polymer ◽  
Scanning Calorimetry ◽  
Molecular Weights ◽  
Scanning Electron

Magnetic nanoparticles used in biomedicine require surface modification ensuring formation of non-toxic, biocompatible nanoparticles. Among the great variety of available biocompatible polymers, a hydrophilic polymer polyethylene glycol (PEG) that has the ability to prevent protein adsorption was chosen for coating prepared magnetite nanoparticles. The aim of this work was to use differential scanning calorimetry (DSC) for studying the adsorption of PEG of different average molecular weights and different feed weights on magnetite nanoparticles and to estimate the maximal amount of PEG adsorbed on the magnetite nanoparticles. The increasing PEG molecular weight has a tendency to the decrease in the maximal feed weight ratio of PEG to magnetite in the studied complex systems. The morphology observed by scanning electron microscopy showed that all studied systems of magnetic particles coated with PEG had almost spherical shape.

Electron Microscope Study of RNA's of Paramyxoviruses

1972 ◽  
Vol 30 ◽  
pp. 196-197
Author(s):  
Ruchama Baum ◽  
J.T. Seto
Keyword(s):  
Electron Microscopy ◽  
Electron Microscope ◽  
Electron Microscope Study ◽  
Sendai Virus ◽  
Sodium Dodecyl ◽  
Rna Molecules ◽  
Virus Particles ◽  
Molecular Weights ◽  
Length Measurements

The ribonucleic acid (RNA) of paramyxoviruses has been characterized by biochemical and physiochemical methods. However, paramyxovirus RNA molecules have not been studied by electron microscopy. The molecular weights of these single-stranded viral RNA molecules are not known as yet. Since electron microscopy has been found to be useful for the characterization of single-stranded RNA, this investigation was initiated to examine the morphology and length measurements of paramyxovirus RNA's.Sendai virus Z strain and Newcastle disease virus (NDV), Milano strain, were used. For these studies it was necessary to develop a method of extracting RNA molecules from purified virus particles. Highly purified Sendai virus was treated with pronase (300 μg/ml) at 37°C for 30 minutes and the RNA extracted by the sodium dodecyl sulfate (SDS)-phenol procedure.

Nucleic Acid Molecules Prepared by Monolayer Techniques

1972 ◽  
Vol 30 ◽  
pp. 178-179
Author(s):  
Dimitrij Lang
Keyword(s):  
Electron Microscopy ◽  
Standard Deviation ◽  
Nucleic Acid ◽  
Cytochrome C ◽  
Nucleic Acids ◽  
Contour Length ◽  
Sample Standard Deviation ◽  
Molecular Weights ◽  
Length Measurements ◽  
Protein Monolayer

The success of the protein monolayer technique for electron microscopy of individual DNA molecules is based on the prevention of aggregation and orientation of the molecules during drying on specimen grids. DNA adsorbs first to a surface-denatured, insoluble cytochrome c monolayer which is then transferred to grids, without major distortion, by touching. Fig. 1 shows three basic procedures which, modified or not, permit the study of various important properties of nucleic acids, either in concert with other methods or exclusively:1) Molecular weights relative to DNA standards as well as number distributions of molecular weights can be obtained from contour length measurements with a sample standard deviation between 1 and 4%.

EXAFS INVESTIGATION OF THE STRUCTURAL SITE OF LIVER ALCOHOL DEHYDROGENASE

1986 ◽  
Vol 47 (C8) ◽  
pp. C8-1165-C8-1168
Author(s):  
M. ZEPPEZAUER ◽  
C. HAAS ◽  
W. MARET ◽  
C. HERMES ◽  
R. F. PETTIFER
Keyword(s):  
Alcohol Dehydrogenase ◽  
Liver Alcohol Dehydrogenase ◽  
Structural Site

scholarly journals Binding of substrate in a ternary complex of horse liver alcohol dehydrogenase.

1982 ◽  
Vol 257 (23) ◽  
pp. 14349-14358 ◽  
Author(s):  
H Eklund ◽  
B V Plapp ◽  
J P Samama ◽  
C I Brändén
Keyword(s):  
Alcohol Dehydrogenase ◽  
Ternary Complex ◽  
Horse Liver Alcohol Dehydrogenase ◽  
Liver Alcohol Dehydrogenase ◽  
Horse Liver
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