de Rham O, Isliker H
Int Arch Allergy Appl Immunol. 1977;55(1-6):61-9. doi: 10.1159/000231910.
Bovine serum IgG1, colostral IgG1 and serum IgG2 with anti-ferritin activity were digested with pepsin or trypsin. Their fragments were characterized by immunoelectrophoresis, gel electrophoresis and gel filtration; their ferritin-binding ability was determined. The kinetics of proteolysis were established by measuring the appearance of free amino groups. No differences were observed between serum and colostrum IgG1. IgG1 was more susceptible to pepsin, and IgG2 to trypsin. This became evident from both the amount of intact IgG determined by gel electrophoresis, immunoelectrophoresis or gel filtration, and from the kinetics of the appearance of amino groups. A model is presented to explain the size, mobilities and properties of the obtained fragments.
具有抗铁蛋白活性的牛血清IgG1、初乳IgG1和血清IgG2用胃蛋白酶或胰蛋白酶进行消化。通过免疫电泳、凝胶电泳和凝胶过滤对其片段进行表征；测定它们与铁蛋白的结合能力。通过测量游离氨基的出现来确定蛋白水解动力学。血清IgG1和初乳IgG1之间未观察到差异。IgG1对胃蛋白酶更敏感，而IgG2对胰蛋白酶更敏感。这从通过凝胶电泳、免疫电泳或凝胶过滤测定的完整IgG量以及氨基出现的动力学中都很明显。提出了一个模型来解释所获得片段的大小、迁移率和性质。
