Wróblewski Z, Mejbaum-Katzenellenbogen W
Acta Biochim Pol. 1984;31(1):17-24.
DEAE-cellulose chromatography was applied for isolation of the complexes of acid alpha 1-glycoprotein (alpha 1-AGP) with immunoglobulins G (IgG). The heterogeneous glycoprotein fraction V was found to contain 75% of total alpha 1-AGP complexed with IgG3, as identified by Protein A-Sepharose chromatography. The results obtained indicate that in normal blood serum 30% of IgG3 and 75% of alpha 1-AGP are bound in the IgG3 - alpha 1-AGP complexes, whereas the remaining parts of IgG3 and alpha 1-AGP are present in free form.
采用二乙氨基乙基纤维素色谱法分离酸性α1-糖蛋白（α1-AGP）与免疫球蛋白G（IgG）的复合物。通过蛋白A-琼脂糖凝胶色谱法鉴定发现，异质性糖蛋白组分V含有与IgG3复合的α1-AGP总量的75%。所得结果表明，在正常血清中，30%的IgG3和75%的α1-AGP以IgG3-α1-AGP复合物的形式结合，而IgG3和α1-AGP的其余部分则以游离形式存在。
