Two-dimensional electrophoresis for the study of blood/serum proteins of the otter, an endangered species

1995 ◽  
Vol 16 (1) ◽  
pp. 1193-1198 ◽  
Author(s):  
Ingrid Miller ◽  
Arno C. Gutleb ◽  
Manfred Gemeiner
1992 ◽  
Vol 13 (1) ◽  
pp. 743-746 ◽  
Author(s):  
Luca Bini ◽  
Barbara Magi ◽  
Carla Cellesi ◽  
Aldo Rossolini ◽  
Vitaliano Pallini

1982 ◽  
Vol 28 (4) ◽  
pp. 759-765 ◽  
Author(s):  
G B Dermer ◽  
L M Silverman ◽  
J F Chapman

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.


1984 ◽  
Vol 30 (12) ◽  
pp. 2021-2025 ◽  
Author(s):  
P Blangarin ◽  
P Deviller ◽  
K Kindbeiter ◽  
J J Madjar

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.


1984 ◽  
Vol 30 (12) ◽  
pp. 1972-1980 ◽  
Author(s):  
J A Daufeldt ◽  
H H Harrison

Abstract In this paper, we present initial quality-control evaluations for a prototype clinical laboratory, recommendations for clinical and technical data record-keeping, and laboratory protocols designed to minimize operator-dependent analytical error in a multi-user environment. These evaluations and recommendations are based on qualitative and semiquantitative two-dimensional electrophoresis studies of the College of American Pathologists' Reference Preparation for Serum Proteins (RPSP). We include the schematic map of RPSP and manually derived estimates of analytical precision for within-run and run-to-run performance with the standard 18 X 18 cm ISO-DALT system.


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