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HLA抗原的共同抗原结构。VII. β2微球蛋白与培养的人细胞系中HLA大分子成分的选择性结合。

Common antigenic structures of HLA antigens. VII. Selective combination binding of beta2-microglobulin with HLA large component in cultured human cell lines.

作者信息

Nakamuro K, Tanigaki N, Pressman D

出版信息

Immunology. 1977 Feb;32(2):139-50.

Abstract

The intracellular distribution of human beta2-microglobulin was examined in human cell lines (a Burkitt lymphoma cell line, a B-lymphoid cell line and an epighelial-like cell line). Freshly harvested cells were mechanically disrupted and separated into the nuclear, cell-membrane and cell-sap fractions. Nearly 90 per cent of the total beta2-microglobulin was recovered in the cell-membrane and cell-sap fractions. The cell-membrane fraction contained 75-88 per cent of the beta2-microglobulin recovered. The rest was in the cell-sap fraction. Most, 84-91 per cent, of the beta2-microglobulin in the cell-membrane fraction was present combined with membrane fraction was present combined with membrane components of about 38,000 daltons that carried the xenoantigenic activity characteristic of the HLA large component. These membrane components did carry HLA alloantigenic activity. No other membrane components were involved in binding beta2-microglobulin. The beta2-microglobulin in the cell-sap fraction was present in the unbound state. Thus, in the cell lines examined, the membrane component which was combined with beta2-microglobulin appeared to be exclusively the HLA large component and no larg excess of beta2-microglobulin over the HLA large component was found.

摘要

在人细胞系(一种伯基特淋巴瘤细胞系、一种B淋巴细胞系和一种上皮样细胞系)中检测了人β2-微球蛋白的细胞内分布。将新鲜收获的细胞机械破碎,分离成细胞核、细胞膜和细胞液部分。几乎90%的总β2-微球蛋白存在于细胞膜和细胞液部分。细胞膜部分含有回收的β2-微球蛋白的75%-88%。其余的在细胞液部分。细胞膜部分中大部分(84%-91%)的β2-微球蛋白与约38000道尔顿的膜成分结合,这些膜成分具有HLA大成分的异种抗原活性特征。这些膜成分确实具有HLA同种抗原活性。没有其他膜成分参与结合β2-微球蛋白。细胞液部分中的β2-微球蛋白以未结合状态存在。因此,在所检测的细胞系中,与β2-微球蛋白结合的膜成分似乎仅为HLA大成分,并且未发现β2-微球蛋白相对于HLA大成分有大量过剩。

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Beta 2-microglobulin: association with lymphocyte receptors.β2-微球蛋白:与淋巴细胞受体的关联
Science. 1973 Dec 28;182(4119):1350-2. doi: 10.1126/science.182.4119.1350.

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