Ohno T, Mesa-Tejada R, Keydar I, Ramanarayanan M, Bausch J, Spiegelman S
Proc Natl Acad Sci U S A. 1979 May;76(5):2460-4. doi: 10.1073/pnas.76.5.2460.
We have shown [Mesa-Tejada, R., Keydar, I., Ramanarayanan, M., Ohno, T., Fenoglio, C. & Spiegelman, S. (1978) Proc. Natl. Acad. Sci. USA 75, 1529--1533] that an antigen immunologically related to gp52, a 52,000-dalton glycoprotein of the mouse mammary tumor virus, can be identified in sections of human breast cancer by means of an indirect immunoperoxidase technique. The specificity of the reaction was established by absorption experiments which revealed that only purified gp52, or material containing it, served to eliminate the IgG molecules responsible for the immunohistochemical reaction in the human breast tumors. We show here that the cross-reactivity between the human and murine tumor antigens is due to the polypeptide rather than the polysaccharide components of gp.52. Sugar-free gp52 prepared by deglycosylation with a mixture of glycosidases was as fully effective as the intact gp52 in removing from anti-MMTV the IgG responsible for the reaction with the human tumor antigen. In contrast, the isolated polysaccharide of gp52 was unable to exert blocking activity.
我们已经证明[梅萨 - 特哈达，R.，凯达尔，I.，拉马纳拉亚南，M.，大野，T.，费诺利奥，C. & 斯皮格尔曼，S.（1978年）《美国国家科学院院刊》75，1529 - 1533]，通过间接免疫过氧化物酶技术，可以在人类乳腺癌切片中鉴定出一种与gp52（小鼠乳腺肿瘤病毒的一种52,000道尔顿糖蛋白）免疫相关的抗原。通过吸收实验确定了反应的特异性，该实验表明只有纯化的gp52或含有它的物质才能消除在人类乳腺肿瘤中负责免疫组织化学反应的IgG分子。我们在此表明，人类和小鼠肿瘤抗原之间的交叉反应性是由于gp52的多肽而非多糖成分。用糖苷酶混合物进行去糖基化制备的无糖gp52在从抗MMTV中去除与人类肿瘤抗原反应的IgG方面与完整的gp52一样有效。相比之下，分离出的gp52多糖没有阻断活性。
