Physicochemical approach to the purification of human alpha1-fetoprotein from the ascites fluid of a hepatoma-bearing patient.
Cancer Res
; 38(1): 6-12, 1978 Jan.
Article
em En
| MEDLINE
| ID: mdl-73414
ABSTRACT
A method for the purification of human alpha1-fetoprotein from the ascites fluid of a hepatoma-bearing patient is described that is capable of yielding large quantities of pure alpha1-fetoprotein within a relatively short period of time. The technique is based entirely on the physicochemical properties of the alpha1-fetoprotein molecule and uses sequential purification steps:
ion-exchange chromatography on DEAE-Sephadex A-50, molecular-sieve chromatography on Sephadex G-200, negative-affinity chromatography on Sepharose-Blue Dextran, positivepaffinity chromatography on concanavalin A-Sepharose and, finally, molecular-sieve chromatography on Sephadex G-100. The efficiency of the entire procedure in its present form is 15% of the alpha1-fetoprotein activity of the starting preparation from ascites fluid. The purity of the final product was shown by polyacrylamide gel electrophoresis, radioimmunoelectrophoresis, and determinations of the NH2-terminal and COOH-terminal amino acid residues of the alphs1-fetoprotein isolated. Amino acid analysis of the final product revealed a composition very similar to those reported for alpha-fetoprotein preparations that have been previously isolated by the use of immunochemical technology.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Alfa-Fetoproteínas
/
Carcinoma Hepatocelular
/
Neoplasias Hepáticas
/
Proteínas de Neoplasias
Limite:
Humans
Idioma:
En
Revista:
Cancer Res
Ano de publicação:
1978
Tipo de documento:
Article