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从血小板中获得的去污剂增溶的HLA抗原的分离及特性

Isolation and properties of detergent-solubilized HLA antigens obtained from platelets.

作者信息

Trägårdh L, Klareskog L, Curman B, Rask L, Peterson P A

出版信息

Scand J Immunol. 1979;9(4):303-14. doi: 10.1111/j.1365-3083.1979.tb03168.x.

DOI:10.1111/j.1365-3083.1979.tb03168.x
PMID:87008
Abstract

Deoxycholate-solubilized HLA antigens have been isolated from platelets and comprised a mixture of 43,000- and 39,000-dalton polypeptide chains associated with beta2-microglobulin. Limited proteolysis experiments suggested that the 39,000-dalton chain is a fragment of the intact 43,000-dalton chain. Further proteolysis of the 39,000-dalton fragment yields a 33,000-dalton component. The 39,000-dalton molecule is more acidic than both the 43,000- and the 33,000-dalton chains. Differences in the amino acid compositions of the 43,000- and 39,000-dalton species demonstrate that the peptide(s) released on generation of the 39,000-dalton component are charged. The proteolytic split most probably occurs in the COOH-terminal end, which, owing to its content of charged amino acids, most probably is not integrated into the hydrocarbon matrix of the membrane. The 39,000- and 43,000-dalton components bind detergent in micellar form and can be incorporated into liposomes. The 33,000-dalton fragment has lost the ability to bind detergent micelles and is not incorporated into liposomes.

摘要

已从血小板中分离出经脱氧胆酸盐增溶的HLA抗原,其由与β2-微球蛋白相关的43,000道尔顿和39,000道尔顿的多肽链混合物组成。有限的蛋白水解实验表明,39,000道尔顿的链是完整的43,000道尔顿链的一个片段。对39,000道尔顿片段的进一步蛋白水解产生一个33,000道尔顿的组分。39,000道尔顿的分子比43,000道尔顿和33,000道尔顿的链酸性更强。43,000道尔顿和39,000道尔顿物种的氨基酸组成差异表明,在产生39,000道尔顿组分时释放的肽是带电荷的。蛋白水解分裂最可能发生在COOH末端,由于其含带电荷的氨基酸,很可能未整合到膜的烃基质中。39,000道尔顿和43,000道尔顿的组分以胶束形式结合去污剂,并可掺入脂质体中。33,000道尔顿的片段已失去结合去污剂胶束的能力,且未掺入脂质体中。

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1
Isolation and properties of detergent-solubilized HLA antigens obtained from platelets.从血小板中获得的去污剂增溶的HLA抗原的分离及特性
Scand J Immunol. 1979;9(4):303-14. doi: 10.1111/j.1365-3083.1979.tb03168.x.
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Detergent solubilization, purification, and separation of specificities of HLA antigens from a cultured human lymphoblastoid line, RPMI 4265.从培养的人淋巴母细胞系RPMI 4265中去污剂增溶、纯化HLA抗原并分离其特异性。
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Common antigenic structures of HL-A antigens. VI. Common antigenic determinants located on the 33,000 Dalton alloantigenic fragment portion of papain-solubilized HL-A molecules.HL-A抗原的共同抗原结构。VI. 位于木瓜蛋白酶可溶解的HL-A分子的33,000道尔顿同种异体抗原片段部分上的共同抗原决定簇。
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Structure of HLA antigens: amino-acid and carbohydrate compositions and NH2-terminal sequences of four antigen preparations.HLA抗原的结构:四种抗原制剂的氨基酸和碳水化合物组成以及氨基末端序列
Proc Natl Acad Sci U S A. 1976 Mar;73(3):910-4. doi: 10.1073/pnas.73.3.910.

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