Morris I G
Immunology. 1969 Jul;17(1):139-49.
The anti- agglutinins of the γG-globulin class in a bovine immune serum chromatographed on DEAE-Sephadex were eluted into two fractions with differing mean electrophoretic mobilities. Although the slower agglutinins were readily transmitted across the gut of young rats fed with these proteins they were detectable in the circulation only as incomplete antibodies; the faster γG-agglutinins were barely transmitted. The transmission characteristics in young rodents of electrophoretic sub-fractions of normal bovine γG-globulin separated by chromatography from a commercial γ-globulin preparation were also studied. This preparation comprised two molecular species of γG-globulins (γ and γ) with distinct mobilities, antigenicities and transmission characteristics. Their mobilities and transmission characteristics were not related. Retrospectively, the slow anti- agglutinins which were readily transmitted in young rats were probably γ-globulins, and the fast agglutinins which were barely transmitted were γ-globulins.
在DEAE-葡聚糖凝胶上进行层析的牛免疫血清中,γG球蛋白类的抗凝集素被洗脱成两个平均电泳迁移率不同的组分。虽然较慢的凝集素很容易通过喂食这些蛋白质的幼鼠肠道,但在循环中仅作为不完全抗体可检测到;较快的γG凝集素几乎不被传递。还研究了从商业γ球蛋白制剂中通过层析分离的正常牛γG球蛋白电泳亚组分在幼龄啮齿动物中的传递特性。该制剂包含两种具有不同迁移率、抗原性和传递特性的γG球蛋白分子种类(γ和γ)。它们的迁移率和传递特性无关。回顾性地看,在幼鼠中容易传递的慢抗凝集素可能是γ球蛋白,而几乎不被传递的快凝集素是γ球蛋白。