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 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.
D002474:Cell-Free System; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006801:Humans; D008970:Molecular Weight; D010920:Placenta / Q000032:analysis*; D010944:Plants / Q000378:metabolism*; D011061:Poly A / Q000378:metabolism; D011247:Pregnancy; D011257:Pregnancy Proteins / Q000096:biosynthesis*; D011268:Pregnancy-Specific beta 1-Glycoproteins / Q000096:biosynthesis*; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000378:metabolism*; D014908:Triticum
D011257:Pregnancy Proteins; D011268:Pregnancy-Specific beta 1-Glycoproteins; D012333:RNA, Messenger; D011061:Poly A