p24 and p26, structurally related cell surface molecules identified by monoclonal antibody BA-2.
p24 and p26, structurally related cell surface molecules identified by monoclonal antibody BA-2.
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p24 和 p26，由单克隆抗体 BA-2 鉴定的结构相关的细胞表面分子。
DOI：
10.1016/0161-5890(85)90007-0
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发表时间：
1985
影响因子：
3.6
通讯作者：
Bradley,JG
中科院分区：
文献类型：
--
作者：
LeBien,TW;Pirruccello,SJ;McCormack,RT;Bradley,JG
本文介绍了额外的结构分析的p24细胞表面分子识别的单克隆抗体BA-2。由于BA-2是广泛的反应与各种正常和恶性淋巴造血和nonlymphohematopoietic细胞，我们研究了不同类型的细胞上表达的p24的结构。从结肠癌细胞、新鲜白血病细胞、白血病细胞系和活化的T细胞中分离的p24的胰蛋白酶肽图谱和二维凝胶电泳表明，p24在检查的细胞内没有表现出结构多态性。正如最近用几种其他细胞表面分子证明的那样，基于[3 H]棕榈酸酯的掺入，显示p24具有共价连接的脂肪酸。我们还发现了一种与p24共沉淀的蛋白质，命名为p26。p26分子不与p24二硫键连接，可以从各种125 I或[35 S]甲硫氨酸标记的细胞中免疫沉淀。V8蛋白酶肽图显示p24和p26在结构上同源。用[35 S]蛋氨酸和内切糖苷酶-F消化的脉冲追踪分析表明，p24和p26可能来自p23前体，但p24和p26之间不存在底物-产物关系。基于这些数据，我们提出p24和p26最有可能是同一基因的差异加工蛋白质产物。
This paper describes additional structural analyses of the p24 cell surface molecule recognized by monoclonal antibody BA-2. Since BA-2 is broadly reactive with a variety of normal and malignant lymphohematopoietic and nonlymphohematopoietic cells, we examined the structure of p24 expressed on different cell types. Tryptic peptide mapping and 2-dimensional gel electrophoresis of p24 isolated from colon carcinoma cells, fresh leukemic cells, leukemic cell lines, and activated T-cells indicated that p24 exhibits no structural polymorphism within the cells examined. As has recently been demonstrated with several other cell surface molecules, p24 is shown 10 possess a covalently-attached fatty acid, based on the incorporation of [3H]palmitate. We have also identified an additional protein, designated p26, that is coprecipitated with p24. The p26 molecule is not disulfide-linked to p24, and can be immunoprecipitated from a variety of125I- or [35S]methionine-labeled cells. V8 protease peptide mapping indicated that p24 and p26 are structurally homologous. Pulse-chase analysis using [35S]methionine and digestion with endoglycosidase-F indicated that p24 and p26 are probably derived from a p23 precursor, but no precursor-product relationship exists between p24 and p26. Based on this data we propose that p24 and p26 are most likely differentially-processed protein products of the same gene.