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At least 667 records · Page 37Linked to original sources
PubMed1990

Strategies for internal amino acid sequence analysis of proteins separated by polyacrylamide gel electrophoresis.

An evaluation has been made of various strategies for obtaining internal amino acid sequence data from electrophoretically separated proteins. Electroblotting, in situ proteolysis and extraction, and direct electroelution are compared. Electroblotting of protein or peptides from gels resulted in poor yields (typically, 1-7%). However, higher yields (3-67%) were achieved by in situ enzymatic cleavage followed by acid extraction of the peptides from the gel. Peptides extracted from the gel were separated by reversed-phase high-performance liquid chromatography (RP-HPLC), on short, small-bore columns (100 x 2.1 mm I.D.), to enable recovery of peptides in small volumes (ca. 50 microliters) suitable for microsequence analysis. Capillary zone electrophoresis under acidic conditions (pH 2.5) was used to assess peptide purity before sequence analysis. Cysteine residues were identified in unmodified proteins or peptides by a characteristic phenylthiohydantoin (PTH)-amino acid derivative during sequence analysis. This derivative does not co-chromatograph with any known PTH-amino acid. Direct electrophoretic elution of protein from gels yielded between 45-50% of applied protein. Proteins recovered from gels by electrophoretic elution required further purification by inverse-gradient RP-HPLC [R. J. Simpson, R. L. Moritz, E. C. Nice and B. Grego, Eur. J. Biochem., 165 (1987) 21] to remove sodium dodecylsulphate and acrylamide-related contaminants for sequence analysis.

Amino Acid Sequence↗
PubMed1996

Large-scale amino-acid analysis for proteome studies.

Amino-acid analysis is a relatively new method for identification of proteins separated by two-dimensional gel electrophoresis and blotted onto polyvinylidene difluoride (PVDF) membranes. This article describes modified amino-acid analysis methods for this purpose. Streamlined sample handling is a key feature of the process. To minimise sample manipulation, a single vial is used for hydrolysis and the protein hydrolysate on PVDF membrane is extracted by a one-step procedure. The hydrolysate should not be stored for long periods before analysis. Applications of the technique are presented to demonstrate the identification procedure. This approach is the most cost-effective and time-effective first step in mass protein screening for a large-scale proteome project.

Amino Acids↗
PubMed1989

Differential oligoclonal band patterns on polyvinyldifluoride membranes.

We report a novel observation which has been reproducibly noted whilst studying immunoglobulin G binding to antigen immobilized on polyvinyldifluoride membranes. In some samples we have observed a difference between the pattern of oligoclonal bands on the front surface when compared to the reverse side of the membrane. We postulate that this observation results from differing affinities of the specific antibody binding to the antigen immobilised on the membrane. High affinity antibody will bind to antigen on the surface of the membrane next to the gel, while lower affinity antibody appears to diffuse through to the reverse side of the membrane.

Antibody Affinity↗
PubMed1991

Affinity purification of antibodies from sera using polyvinylidenedifluoride (PVDF) membranes as coupling matrices for antigens presented by autoantibodies to triosephosphate isomerase.

Polyvinylidenedifluoride (PVDF) membranes covered with antigen can be used for affinity purification of antibodies from sera. These antibodies serve as an appropriate substitute for monoclonal antibodies when performing cytological and analytical experiments with the respective antigen. The usefulness of this method is demonstrated with the purification of IgM autoantibodies produced against human triosephosphate isomerase in acute Epstein-Barr virus infection. Compared with the original serum, the specific activity of the purified antibodies was up to 1400-fold higher, and the recovery of the anti-triosephosphate isomerase activity between 25 and 33%.

Animals↗