Isolation and amino terminal sequencing of a novel melanoma-associated antigen.
Isolation and amino terminal sequencing of a novel melanoma-associated antigen.
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DOI：
10.1016/0003-9861(85)90241-3
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发表时间：
1985-11
影响因子：
3.9
通讯作者：
A. Ross;B. Dietzschold;D. Jackson;J. Earley;B. Ghrist;B. Atkinson;H. Koprowski
中科院分区：
文献类型：
--
作者：
A. Ross;B. Dietzschold;D. Jackson;J. Earley;B. Ghrist;B. Atkinson;H. Koprowski
描述了黑色素瘤相关糖蛋白抗原的生化特征，其表达取决于肿瘤进展阶段和黑素细胞分化。这种抗原是用免疫过氧化物酶染色黑色素瘤细胞的单抗鉴定的，它被合成为30,000-6万-Da的唾液酸糖蛋白前体。该抗原的双向凝胶电泳法分离了20多种形式，在电荷和分子质量上都是不同的。翻译后加工的动力学、加工对衣霉素的敏感性和寡糖链的相对分子质量表明寡糖是N-键的。对通过免疫亲和层析和高压液相色谱或聚丙烯酰胺凝胶电泳法纯化的抗原进行氨基酸序列测定，可以指定前20个氨基酸。
The biochemical characteristics are described for a melanoma-associated glycoprotein antigen, whose expression depends on stage of tumor progression and melanocytic differentiation. This antigen, identified using a monoclonal antibody which specifically stains melanoma cells in immunoperoxidase assay of fixed tissue sections, is synthesized as a 30,000-Da precursor and then processed to a 30,000- to 60,000-Da sialylated glycoprotein. Two-dimensional gel electrophoresis of the antigen resolved more than 20 forms, heterogeneous in both charge and molecular weight. The kinetics of post-translational processing, the sensitivity of processing to tunicamycin, and the molecular weight of the oligosaccharide chains indicate that the oligosaccharides are N-linked. Amino acid sequencing of the antigen purified by immunoaffinity chromatography and by highpressure liquid chromatography or polyacrylamide gel electrophoresis allowed the assignment of the first 20 acids.