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

FEBS Letters

Giuliani, C.¹  Iacobelli, S.²  D'Egidio, M.²  Natoli, C.²  Schlessinger, J.³  Rubistein, M.³  Bucci, I.¹  Tinari, N.² 

[1] Cattedra di Endocrinologia, Universita degli Studi ‘G. D'Annunzio’, Chieti, Italy;Cattedra Oncologia Medica, Universita degli Studi ‘G. D'Annunzio’, Chieti, Italy;Dept. of Pharmacology, New York University, New York, NY, USA

关键词: Tumor-associated antigen;    Monoclonal antibody;    Breast cancer;    Protein purification;    NH2-terminal amino acid sequence;    BSA;    bovine serum albumin;    ELISA;    enzyme-linked immunosorbent assay;    IRMA;    immunoradiometric assay;    mAb;    monoclonal antibody;    NP-40;    Nonidet P-40;    PAGE;    polyacrylamide gel electrophoresis;    PBS;    phosphate-buffered saline;    SDS;    sodium dodecyl sulfate;   

DOI  :  10.1016/0014-5793(93)80037-U

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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-tenninal amino acid sequence revealed no homology to known protein.

【 授权许可】

Unknown