Griffiths B W, Godard A
J Reprod Immunol. 1981 Jun;3(2):131-6. doi: 10.1016/0165-0378(81)90017-6.
The structure of a high-molecular-weight form of Pregnancy-Specific beta 1-Glycoprotein designated PSB1G-I that had been previously isolated from maternal serum was studied by gel chromatography in guanidine hydrochloride dissociating solvent. Evidence was obtained that subunits of identical size (bonded together non-covalently) but of differing polypeptide compositions constitute the PSB1G-I molecule. The subunits of PSB1G-I have been designated alpha and beta subunits. Reduction of PSB1G-I results in an intact alpha chain and two beta chains (beta 1 and beta 2) that are linked in the parent beta subunit by covalent bonds. The collective molecular weights of the alpha, beta 1 and beta 2 chains are equal to 97 800 which is assumed to represent the 'true' molecular weight of 'native' serum PSB1G.
通过在盐酸胍解离溶剂中进行凝胶色谱法，对先前从母体血清中分离出的一种高分子量形式的妊娠特异性β1-糖蛋白（称为PSB1G-I）的结构进行了研究。有证据表明，大小相同（通过非共价键结合在一起）但多肽组成不同的亚基构成了PSB1G-I分子。PSB1G-I的亚基被命名为α亚基和β亚基。PSB1G-I的还原产生一条完整的α链和两条β链（β1和β2），它们在母体β亚基中通过共价键相连。α、β1和β2链的总分子量等于97800，这被认为代表了“天然”血清PSB1G的“真实”分子量。
