![]() | Only 14 pages are availabe for public view |
Abstract Schwangerschafts protein 1 ( SP1) is a glycoprotein secreted by the placenta. It the specific to pregnancy and its exact function is not known. In the present work, (sp1) was isolated and purified from human full term placentae. It was found that only two antigen populations with sp1 determinants could be detected. The larger molecule sp1 a – with a molecular weight of 430 kd as determined by gel filtration. The smaller protein, sp1B was of 90 kd. The two proteins were purified from the crude placental extract by gel filtration, ion exchange and protein elution from the polyacrylamide gel. The purified a – from was 95% pure while for the B from , the purity was 100%. The whole method is simple and cheap. It has an overall yield of 45% and resulted in 952 fold purification for sp1a- and 544 fold for sp1B- . Pure sp1a- and sp1B staining for glycoprotein showed that they are glycoprotein in nature. The glycoprotein staining of cleaved sp1a- and sp1B- showed carbohydrate side chain at 36 kd in both forms. |