Borucinska J D, Ayoub I, Garmendia A E
Northeastern Research Center for Wildlife Diseases, Department of Pathobiology, University of Connecticut, Storrs 06268, USA.
J Wildl Dis. 1996 Oct;32(4):687-90. doi: 10.7589/0090-3558-32.4.687.
Muskrat (Ondatra zibethicus) immunoglobulin fraction was separated from whole serum by Protein A Sepharose chromatography. In serum electrophoresis, this fraction had a gamma motility; when electrophoresed on a polyacrylamide gel with sodium dodecyl sulfate it resolved into two protein bands of approximately 52 and 25 kilodaltons, respectively. These bands were consistent with molecular weights of known heavy and light chains of immunoglobulin G (IgG) in other closely related species. Furthermore, the putative muskrat immunoglobulins had a strong cross-reactivity with mouse IgG1, IgG3, and kappa chain in an enzyme-linked immunosorbent assay. We propose, that the proteins bound to the Protein A Sepharose represent muskrat immunoglobulins of the IgG class.
通过蛋白A琼脂糖凝胶柱色谱法从麝鼠（Ondatra zibethicus）全血清中分离出免疫球蛋白组分。在血清电泳中，该组分具有γ迁移率；当在含有十二烷基硫酸钠的聚丙烯酰胺凝胶上进行电泳时，它分别分解为两条分子量约为52和25千道尔顿的蛋白带。这些条带与其他密切相关物种中已知的免疫球蛋白G（IgG）重链和轻链的分子量一致。此外，在酶联免疫吸附测定中，推定的麝鼠免疫球蛋白与小鼠IgG1、IgG3和κ链具有强烈的交叉反应性。我们提出，与蛋白A琼脂糖凝胶结合的蛋白质代表IgG类的麝鼠免疫球蛋白。
