Two-dimensional electrophoresis analysis of human serum proteins during the acute-phase response

1992 ◽  
Vol 13 (1) ◽  
pp. 743-746 ◽  
Author(s):  
Luca Bini ◽  
Barbara Magi ◽  
Carla Cellesi ◽  
Aldo Rossolini ◽  
Vitaliano Pallini
Keyword(s):  
Human Serum ◽  
Acute Phase ◽  
Acute Phase Response ◽  
Serum Proteins ◽  
Phase Response ◽  
Two Dimensional ◽  
Two Dimensional Electrophoresis ◽  
Dimensional Electrophoresis ◽  
Human Serum Proteins

Two-dimensional electrophoresis of human serum proteins modified by ampicillin during therapeutic treatment

1995 ◽  
Vol 16 (1) ◽  
pp. 1190-1192 ◽  
Author(s):  
Barbara Magi ◽  
Barbara Marzocchi ◽  
Luca Bini ◽  
Carla Cellesi ◽  
Aldo Rossolini ◽  
...  
Keyword(s):  
Human Serum ◽  
Serum Proteins ◽  
Two Dimensional ◽  
Therapeutic Treatment ◽  
Two Dimensional Electrophoresis ◽  
Dimensional Electrophoresis ◽  
Human Serum Proteins

Two-dimensional electrophoretic patterns of acute-phase human serum proteins in the course of bacterial and viral diseases

1996 ◽  
Vol 17 (3) ◽  
pp. 612-616 ◽  
Author(s):  
Luca Bini ◽  
Barbara Magi ◽  
Barbara Marzocchi ◽  
Carla Cellesi ◽  
Brunilde Berti ◽  
...  
Keyword(s):  
Human Serum ◽  
Acute Phase ◽  
Serum Proteins ◽  
Viral Diseases ◽  
Two Dimensional ◽  
Electrophoretic Patterns ◽  
Human Serum Proteins

Two-dimensional electrophoresis of proteins in human serum: improved resolution by use of narrow pH gradients and prolonged electrophoresis.

1984 ◽  
Vol 30 (12) ◽  
pp. 2008-2013 ◽  
Author(s):  
T Marshall ◽  
K M Williams ◽  
O Vesterberg
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Human Serum ◽  
Serum Proteins ◽  
Sodium Dodecyl ◽  
Staining Procedure ◽  
Two Dimensional ◽  
Ph Gradients ◽  
Two Dimensional Electrophoresis ◽  
Dodecyl Sulfate ◽  
Dimensional Electrophoresis

Abstract The limited resolution of serum proteins achieved with a simplified technique of two-dimensional electrophoresis (Clin. Chim. Acta 103: 51-59, 1980) has been improved by using different ampholyte (Ampholine) mixtures in the first dimension, to obtain relatively shallow pH gradients, and prolonged electrophoresis time in the second dimension. The technique has been further simplified, without negative effect, by decreasing the concentration of non-ionic detergent (first dimension), omitting both sodium dodecyl sulfate equilibration and the use of a stacking gel (second dimension), and by using an improved silver-staining procedure. Reverse-polarity isoelectric focusing and non-equilibrium pH-gradient electrophoresis have been successfully used to resolve the basic polypeptides in serum after deleting sodium dodecyl sulfate from the sample preparation. These combined techniques reveal over 1100 polypeptides in human serum. After immunodeletion of albumin, additional serum polypeptides are seen. Immunodeletion of serum proteins from plasma reveals polypeptides that are relatively specific to plasma.

Enhancement techniques for detecting trace and fluid-specific components in two-dimensional electrophoresis patterns.

1982 ◽  
Vol 28 (4) ◽  
pp. 759-765 ◽  
Author(s):  
G B Dermer ◽  
L M Silverman ◽  
J F Chapman
Keyword(s):  
Cerebrospinal Fluid ◽  
Serum Proteins ◽  
Prostatic Acid Phosphatase ◽  
Two Dimensional ◽  
Cibacron Blue ◽  
Two Dimensional Electrophoresis ◽  
Prostatic Fluid ◽  
Creatine Kinase B ◽  
Malignant Effusions ◽  
Dimensional Electrophoresis

Abstract Albumin and other serum-derived proteins were removed from several types of body fluids by affinity chromatography, to facilitate detection of trace or non-serum-derived proteins in two-dimensional electrophoresis patterns. Albumin was removed by the dye Cibacron Blue F3G-A coupled to Sepharose. Two-dimensional patterns of albumin-depleted serum lack the large albumin spot, and several families of spots become visible that ordinarily are partly or totally hidden by it. However, other proteins also bind to Cibacron Blue. Most serum proteins, including albumin, were effectively removed by anti-human serum antibodies coupled to Sepharose. Two-dimensional patterns of serum-depleted cerebrospinal fluid exhibit five clusters of probable nervous-system protein families not detected in serum. One additional family, probably antigenically related to transferrin, was removed by the affinity step. Two-dimensional patterns of serum-depleted prostatic fluid exhibit five major non-serum families, two of which may be creatine kinase B subunits and prostatic acid phosphatase. Two-dimensional patterns of serum-depleted malignant effusions exhibit one or more of three proteins that possibly are tumor products. Pattern matching suggests the presence of one non-serum-derived protein family common to cerebrospinal fluid, prostatic fluid, and malignant effusions. Prostatic fluid and malignant effusions have in common as many as three non-serum families of proteins.

Gamma heavy chain disease studied by two-dimensional electrophoresis and immuno-blotting techniques.

1984 ◽  
Vol 30 (12) ◽  
pp. 2021-2025 ◽  
Author(s):  
P Blangarin ◽  
P Deviller ◽  
K Kindbeiter ◽  
J J Madjar
Keyword(s):  
Heavy Chain ◽  
Monoclonal Gammopathy ◽  
Serum Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Two Dimensional ◽  
Two Dimensional Electrophoresis ◽  
Disease Protein ◽  
Dimensional Mapping ◽  
Dimensional Electrophoresis ◽  
Heavy Chain Disease

Abstract We used two-dimensional polyacrylamide gel electrophoresis and immunoblotting techniques to study serum proteins from a patient with a monoclonal gammopathy. Two-dimensional electrophoresis was optimized for serum proteins with two main goals: (a) to allow the resolution of many serum proteins in both directions, with penetration of the maximum number of proteins in the first dimension; and (b) to obtain the best reproducibility from one experiment to another, within the limits of the current technique. These analyses, combined with immunoblotting, permitted us to characterize a gamma heavy chain disease protein of 34 000-Da molecular mass. Moreover, two-dimensional mapping of the patient's serum proteins allowed demonstration of the microheterogeneity of this monoclonal component.

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