PURIFICATION AND CHARACTERIZATION OF A 90-KDA PROTEIN RELEASED FROM HUMAN TUMORS AND TUMOR-CELL LINES
PURIFICATION AND CHARACTERIZATION OF A 90-KDA PROTEIN RELEASED FROM HUMAN TUMORS AND TUMOR-CELL LINES
复制标题
DOI：
10.1016/0014-5793(93)80037-u
复制
发表时间：
1993-03-15
期刊：
影响因子：
3.5
通讯作者：
SCHLESSINGER, J
中科院分区：
文献类型：
--
作者：
IACOBELLI, S;BUCCI, I;SCHLESSINGER, J
从乳腺癌患者血清、卵巢癌腹水和人乳腺癌细胞条件培养液中纯化出一种新的肿瘤相关蛋白，命名为90K，可被单抗SP-2识别。在这三个来源中，天然90K以高分子量复合体的形式存在，该复合体被SDS-PAGE解离成约90,000 Da的主带。根据电泳迁移率、浮力密度值、氨基酸组成和免疫反应性，来自不同来源的90K似乎是相同的。NH2-末端氨基酸序列与已知蛋白质没有同源性。
A novel tumor-associated protein, termed 90K, and recognized by mAb SP-2 was purified from serum of breast cancer patients, ovarian cancer ascitic fluid and conditioned medium of human breast cancer cells. In these three sources, native 90K is present as a high molecular weight complex that was dissociated by SDS-PAGE into a major band of approximately 90,000 Da. On the basis of electrophoretic mobility, buoyant density value, amino acid composition, and immunoreactivity, the 90K from the different sources appeared to be identical. NH2-terminal amino acid sequence revealed no homology to known protein.