Brown P J, Evans J P, Sinor L T, Tilzer L T, Plapp F V
Am J Pathol. 1983 Feb;110(2):127-34.
Previous studies on the human Rhesus D antigen revealed several similarities between the D antigen and proteolipids. Proteolipids are a family of low-molecular-weight, hydrophobic proteins that are soluble in chloroform/methanol. In addition, many proteolipids bind dicyclohexylcarbodiimide (DCCD), an ATPase inhibitor. For determination of whether the D antigen was a proteolipid, the chloroform/methanol solubility and DCCD binding of the antigen were investigated. DCCD specifically inhibited the binding of anti-D IgG to Rh-positive red blood cells and to partially purified D antigen as determined by enzyme-linked immunoassays. The antigen was not only soluble in chloroform/methanol but was purified to apparent homogeneity by extraction with these solvents and subsequent discontinuous sucrose gradient centrifugation. The antigen's chloroform/methanol solubility, DCCD binding, low molecular weight, and previously reported phospholipid dependence allow classification of the D antigen as a proteolipid. The discovery that the D antigen is a proteolipid provides further clues to the antigen's cellular function.
先前对人类恒河猴D抗原的研究揭示了D抗原与蛋白脂质之间的若干相似之处。蛋白脂质是一类低分子量的疏水蛋白，可溶于氯仿/甲醇。此外，许多蛋白脂质可结合二环己基碳二亚胺（DCCD），一种ATP酶抑制剂。为了确定D抗原是否为蛋白脂质，研究了该抗原的氯仿/甲醇溶解性和与DCCD的结合情况。通过酶联免疫测定法确定，DCCD可特异性抑制抗-D IgG与Rh阳性红细胞以及部分纯化的D抗原的结合。该抗原不仅可溶于氯仿/甲醇，还通过用这些溶剂萃取并随后进行不连续蔗糖梯度离心纯化至表观均一性。该抗原的氯仿/甲醇溶解性、与DCCD的结合、低分子量以及先前报道的对磷脂的依赖性使得D抗原可被归类为蛋白脂质。D抗原是蛋白脂质这一发现为该抗原的细胞功能提供了进一步线索。
