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从人肿瘤及肿瘤细胞系中释放的一种90 kDa蛋白的纯化与特性分析

Purification and characterization of a 90 kDa protein released from human tumors and tumor cell lines.

作者信息

Iacobelli S, Bucci I, D'Egidio M, Giuliani C, Natoli C, Tinari N, Rubistein M, Schlessinger J

机构信息

Cattedra Oncologia Medica, Università degli Studi G. D'Annunzio, Chieti, Italy.

出版信息

FEBS Lett. 1993 Mar 15;319(1-2):59-65. doi: 10.1016/0014-5793(93)80037-u.

DOI:10.1016/0014-5793(93)80037-u
PMID:8454062
Abstract

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.

摘要

一种名为90K的新型肿瘤相关蛋白,可被单克隆抗体SP-2识别,从乳腺癌患者血清、卵巢癌腹水和人乳腺癌细胞条件培养基中纯化得到。在这三种来源中,天然90K以高分子量复合物形式存在,经SDS-PAGE解离后形成一条约90,000 Da的主要条带。基于电泳迁移率、浮力密度值、氨基酸组成和免疫反应性,不同来源的90K似乎是相同的。氨基末端氨基酸序列与已知蛋白无同源性。

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