Isolation of human alpha-fetoprotein in two fractionation steps and demonstration of homogeneity
| Autor: | S. Y. Lee, K. H. Kortright, G. G. Kapadia, T. A. Waldmann, K. R. McINTIRE |
|---|---|
| Rok vydání: | 1979 |
| Předmět: |
Gel electrophoresis
Two-dimensional gel electrophoresis Chromatography Chemistry Isoelectric focusing Protein Conformation Gel electrophoresis of proteins Buffers Biochemistry Chromatography Affinity Molecular Weight chemistry.chemical_compound Isoelectric point Molecular-weight size marker Genetics Humans Electrophoresis Polyacrylamide Gel Isoelectric Point alpha-Fetoproteins Sodium dodecyl sulfate Isoelectric Focusing Polyacrylamide gel electrophoresis |
| Zdroj: | Preparative biochemistry. 9(2) |
| ISSN: | 0032-7484 |
| Popis: | Human alpha-fetoprotein (hAFP) has been isolated from cord serum in 40% yield using an isolation procedure consisting of only two major steps: affinity chromatography followed by preparative polyacrylamide gel electrophoresis (PAGE). The final product appeared homogeneous on the basis of five independent criteria for purity. Sodium dodecyl sulfate gel electrophoresis (SDS-PAGE) demonstrated a single polypeptide chain with molecular weight of 71,000. The protein exhibited an apparent isoelectric point (pI') of 4.85, molecular radius of 3.0 nm and a valence (net H+/molecule) of 21.9 derived from computation of analytical PAGE data. The two-step isolation procedure made it possible for a single operator to isolate milligram amounts of hAFP in a matter of weeks. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|