| Autor: |
Bocco, J., Actis, A., Flury, A., Patrito, L. |
| Zdroj: |
Molecular Biology Reports; Mar1987, Vol. 12 Issue 1, p55-59, 5p |
| Abstrakt: |
Poly (A)-mRNA obtained from human term placenta using guanidine HCl and oligo (dT) cellulose chromatography was translated in a wheat germ cell-free system. SDS-polyacrylamide gel electrophoresis analysis of the translation products revealed the presence of several polypeptides with molecular weights ranging from 10 KD to 70 KD. A single protein band representing around 1% of the total radioactive proteins synthesized in the presence of 2.5 μg of mRNA was isolated by immunoprecipitation, using specific antiserum against either the native 'Pregnancy-specific β-glycoprotein' or a reduced and carboxymethylated derivative. The molecular weight of 31-2 KD of this translation product corresponding to the nonprocessed precursor could account for the 43 KD value assigned to the protein purified from human pregnant serum. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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