Identification and molecular weight of SP1 synthesized from mRNA of human placenta in a wheat germ cell-free system

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 weigh...

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Bibliographic Details
Published in:Molecular biology reports 1987, Vol.12 (1), p.55-59
Main Authors: BOCCO, J. L, ACTIS, A, FLURY, A, PATRITO, L. C
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Cell-Free System
Electrophoresis, Polyacrylamide Gel
Female
Fundamental and applied biological sciences. Psychology
Glycoproteins
Humans
Molecular Weight
Placenta - analysis
Plants - metabolism
Poly A - metabolism
Pregnancy
Pregnancy Proteins - biosynthesis
Pregnancy-Specific beta 1-Glycoproteins - biosynthesis
Protein Biosynthesis
Proteins
RNA, Messenger - metabolism
Triticum
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Summary: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 micrograms of mRNA was isolated by immunoprecipitation, using specific antiserum against either the native 'Pregnancy-specific beta 1-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 form human pregnant serum.
ISSN:0301-4851
1573-4978
DOI:10.1007/BF00580651