Analysis of virus protein heterogeneity among group B coxsackie viruses using a “mini” two-dimensional gel electrophoresis system

1989 ◽  
Vol 10 (11) ◽  
pp. 793-800 ◽  
Author(s):  
Phillip Cash
Keyword(s):  
Gel Electrophoresis ◽  
Virus Protein ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Electrophoresis System ◽  
Group B

Two-dimensional gel electrophoresis of human brain proteins. I. Technique and nomenclature of proteins.

1982 ◽  
Vol 28 (4) ◽  
pp. 782-789 ◽  
Author(s):  
D E Comings
Keyword(s):  
Human Brain ◽  
Gel Electrophoresis ◽  
Urea Solution ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Polypeptide Patterns ◽  
Normal Individuals ◽  
Molecular Masses ◽  
Group B ◽  
The Individual

Abstract To understand at a molecular level the basis of the normal and pathological genetic differences between individuals it is necessary to begin a detailed two-dimensional gel electrophoretic mapping of the proteins of the human brain in normal individuals and those with various genetic neurological disorders. The present study is an examination of the polypeptide patterns of extracts of the human brain made with 9 mol/L urea solution. Details of the technique and the nomenclature of the patterns obtained are presented. the gels are separated into 20 sub-sections, based on standards with known molecular masses and isoelectric points. Groups of polypeptides within these sub-sections are identified by a number and a letter; the individual proteins are identified by a number. Thus, protein 1 in subsection 8, group b, would be designated 8b: 1. Subsequent papers in this series identify many of these proteins; show which proteins belong to the cytosol, synaptosome, myelin, and other brain fractions; show how these patterns vary between normal individuals and those with different neurological and psychiatric conditions; examine the effect of severe gliosis; and present the results of non-equilibrium gel electrophoresis for the more basic proteins.

Evaluation of antibody drugs using automated two dimensional gel electrophoresis system

2018 ◽  
Vol 62 (1) ◽  
pp. 13-18
Author(s):  
Hideki Kinoshita ◽  
Masayuki Kosugi ◽  
Kimihiko Yabe ◽  
Takateru Matsunaga ◽  
Mitsuhiro Kinoshita
Keyword(s):  
Gel Electrophoresis ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Electrophoresis System

Two-dimensional gel electrophoresis of serum specimens from patients with monoclonal gammopathies.

1982 ◽  
Vol 28 (4) ◽  
pp. 900-907 ◽  
Author(s):  
R P Tracy ◽  
R M Currie ◽  
R A Kyle ◽  
D S Young
Keyword(s):  
Gel Electrophoresis ◽  
Light Chains ◽  
Correct Identification ◽  
Two Dimensional ◽  
Excellent Correlation ◽  
Serum Samples ◽  
Two Dimensional Gel Electrophoresis ◽  
Monoclonal Gammopathies ◽  
Heavy Chains ◽  
Electrophoresis System

Abstract We modified the ISO-DALT two-dimensional gel electrophoresis system to allow the routine examination of serum specimens from patients with monoclonal gammopathies. This system, MC-Iso 1, is characterized by a broad pH gradient for resolving the basic immunoglobulin heavy and light chains. The increased resolution of basic proteins may be explained on theoretical grounds by an increase in voltage in this region of the cell. Ancillary techniques, such as those for albumin removal and pI assignment through use of charge standards, have also been implemented. The locations of immunoglobulin heavy chains have been confirmed by examination of over 250 serum samples as well as by "electro-blotting," with use of specific antisera. IgG subclass may also be predicted by location, but not with perfect accuracy. Differentiation of kappa and lambda light chains by relative mobility has been examined; the predictive value for correct identification of kappa chains is 83%, that for lambda chains 69%. Several unknown proteins have been observed in macroglobulinemia, related to mu heavy chain. Finally, we have determined that there is excellent correlation between non-denaturing isoelectric focusing and our system for pI assignment of light chains. This has importance due to reports of the potential importance of light-chain pI in the development of renal disease in patients with monoclonal gammopathies.

The TYCHO system for computer analysis of two-dimensional gel electrophoresis patterns.

1981 ◽  
Vol 27 (11) ◽  
pp. 1807-1820 ◽  
Author(s):  
N L Anderson ◽  
J Taylor ◽  
A E Scandora ◽  
B P Coulter ◽  
N G Anderson
Keyword(s):  
Background Subtraction ◽  
Gel Electrophoresis ◽  
High Speed ◽  
Quantitative Measurement ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Two Dimensional Electrophoresis ◽  
Spot Detection ◽  
Electrophoresis System ◽  
Dimensional Electrophoresis

Abstract We describe here a computer system for the analysis of high-resolution two-dimensional gel-electrophoresis patterns, with some initial applications. The system (called TYCHO) comprises programs for image acquisition, background subtraction and smoothing, spot detection, gaussian spot modeling, and pattern matching and comparison. It is based on a conventional minicomputer, but makes extensive use of a high-speed array processor in the image-processing and -modeling steps. Used in concert with the ISO-DALT two-dimensional electrophoresis system (Anal. Biochem. 85:331-354, 1978), TYCHO allows quantitative measurement of hundreds of proteins in complex biological samples, and constitutes the initial data-reduction system required for work towards a Human Protein Index.

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