Bocco J L, Actis A, Flury A, Patrito L C
Mol Biol Rep. 1987;12(1):55-9. doi: 10.1007/BF00580651.
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.
使用盐酸胍和寡聚（dT）纤维素色谱法从人足月胎盘获得的聚（A+）-mRNA在麦胚无细胞系统中进行翻译。对翻译产物进行SDS-聚丙烯酰胺凝胶电泳分析，结果显示存在几种分子量在10 KD至70 KD之间的多肽。通过免疫沉淀法，使用针对天然“妊娠特异性β1-糖蛋白”或还原和羧甲基化衍生物的特异性抗血清，分离出一条单一蛋白带，该蛋白带约占在2.5微克mRNA存在下合成的总放射性蛋白的1%。这种对应于未加工前体的翻译产物的分子量为31 - 2 KD，这可以解释从人妊娠血清中纯化的该蛋白所赋予的43 KD值。
