MOLECULAR-STRUCTURE OF HUMAN HISTOCOMPATIBILITY ANTIGENS - HLA-C SERIES
MOLECULAR-STRUCTURE OF HUMAN HISTOCOMPATIBILITY ANTIGENS - HLA-C SERIES
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DOI：
10.1002/eji.1830070816
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发表时间：
1977-01-01
影响因子：
5.4
通讯作者：
CRUMPTON, MJ
中科院分区：
文献类型：
--
作者：
SNARY, D;BARNSTABLE, CJ;CRUMPTON, MJ
通过各种标准判断，B [骨髓衍生的]淋巴母细胞样细胞系BRI 8的HLA-CW 2抗原在结构上与HLA-A和B抗原同源。每种抗原包含与β 2-微球蛋白（β 2 m）非共价结合的43，000 MW的糖基化多肽。揭示了分子参数的一些小的差异。脱氧胆酸盐溶解的HLA-CW 2抗原以与HLA-A抗原相同的速率沉降，但比HLA-B抗原的速率略快。这种变化显然是由于结合的脱氧胆酸盐的量不同。尽管基本上所有的HLA-A和B抗原以及大约一半的HLA-CW 2抗原被透镜culinaris凝集素-琼脂糖凝胶强烈吸附，但剩余的HLA-CW 2抗原的结合要弱得多，并且不需要糖来洗脱。这种差异反映了HLA-CW 2抗原的碳水化合物部分的一些结构异质性。HLA-CW 2抗原的表达明显低于HLA-A或B抗原。BRI 8质膜的基本上所有β 2 m可能与HLA-A、B和C同种异体抗原多肽相关。
The HLA-CW2 antigen of the B [bone marrow-derived] lymphoblastoid cell line BRI 8 is structurally homologous to the HLA-A and B antigens as judged by various criteria. Each antigen comprised a glycosylated polypeptide of 43,000 MW that is noncovalently associated with .beta.2-microglobulin (.beta.2m). Some small differences in molecular parameters were revealed. The deoxycholate-solubilized HLA-CW2 antigen sedimented at the same rate as the HLA-A antigens but at a slightly faster rate than the HLA-B antigens. This variation is apparently due to different amounts of bound deoxycholate. Whereas essentially all of the HLA-A and B antigens and about half of the HLA-CW2 antigen were strongly adsorbed by Lens culinaris lectin-Sepharose, the remaining HLA-CW2 antigen was bound much more weakly and did not require sugar for elution. This difference reflects some structural heterogeneity in the carbohydrate moiety of the HLA-CW2 antigen. The HLA-CW2 antigen is apparently expressed to a lower extent than the HLA-A or B antigens. Essentially all of the .beta.2m of the BRI 8 plasma membrane is probably associated with the HLA-A, B and C alloantigenic polypeptides.