Bovine IgG can aggregate at conditions simulating pasteurization and binds to some human Fc gamma receptors.
Bovine IgG can aggregate at conditions simulating pasteurization and binds to some human Fc gamma receptors.
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牛 IgG 可以在模拟巴氏灭菌的条件下聚集并与一些人 Fc γ 受体结合。
DOI：
10.1016/0161-5890(87)90144-1
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发表时间：
1987
影响因子：
3.6
通讯作者：
KulczyckiJr,A
中科院分区：
文献类型：
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作者：
KulczyckiJr,A
研究了牛 IgG 制剂与各种不同的人白细胞 Fcγ 受体结合的能力。在使用完整细胞和分离的 Fcγ 受体的实验中，证明牛 IgG 可以与四种人类细胞类型的 Fcγ 受体结合，但不能与人中性粒细胞的 Fcγ 受体结合。在人 IgG-Sepharose 柱上从人 B 和 T 淋巴细胞、单核细胞和嗜酸性粒细胞中纯化的 125 I 标记的 Fcγ 受体能够与不溶性牛 IgG 特异性重新结合。相比之下，放射性碘标记的人中性粒细胞 Fcγ 受体不会与牛 IgG-Sepharose 重新结合。在125 I标记的热聚集牛IgG与各种人类白细胞群的结合的研究中证明了类似的特异性模式。标记的聚集牛 IgG 与外周血单核细胞、慢性淋巴细胞白血病患者的 B 细胞和巨噬细胞样 U-937 细胞结合，但与正常人粒细胞的结合较差。标记的非聚集牛 IgG 未明显与任何细胞群结合。由于膳食来源中的牛 IgG 经常暴露于热量，因此检查了加热对牛 IgG 的物理状态和 Fc 结合特性的影响。数据显示，将浓度为 0.9–3.6 mg/ml 的牛 IgG 在中性缓冲液中于 63°C 加热 30 分钟，会导致牛免疫球蛋白聚集（聚集 10–16%），并增加牛 IgG 制剂与完整细胞的人 Fcγ 受体结合的能力。凝胶过滤研究表明，牛 IgG 也可能在生奶巴氏灭菌过程中聚集。
The ability of bovine IgG preparations to bind to the various distinct human leukocyte Fcγreceptors was studied. In experiments using intact cells and isolated Fcγreceptors, it was demonstrated that bovine IgG can bind to Fcγreceptors of four human cell types but not to Fcγreceptors of human neutrophils.125I-labeled Fcγreceptors purified on human IgG-Sepharose columns from human B and T lymphocytes, monocytes and eosinophils were able to rebind specifically to insolubilized bovine IgG. In contrast, radioiodinated human neutrophil Fcγreceptors did not rebind to bovine IgG-Sepharose. A similar pattern of specificity was demonstrated in studies of the binding of125I-labeled heat-aggregated bovine IgG to various human leukocyte populations. The labeled aggregated bovine IgG bound to peripheral blood mononuclear cells, to B cells from chronic lymphocytic leukemia patients and to macrophage-like U-937 cells, but bound poorly to normal human granulocytes. Labeled non-aggregated bovine IgG was not appreciably bound to any of the cell populations. Since bovine IgG in dietary sources is frequently exposed to heat, the effect of heating on the physical state and Fc-binding properties of bovine IgG was examined. The data show that heating bovine IgG at concns of 0.9–3.6 mg/ml at 63°C for 30 min in neutral buffer causes aggregation of bovine immunoglobulin (10–16% aggregation) and increases the ability of bovine IgG preparations to bind to human Fcγreceptors of intact cells. Gel filtration studies suggest the possibility that bovine IgG may also be aggregated during the pasteurization of raw milk.