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PARTIAL PURIFICATION AND CHARACTERIZATION OF AN AUTOCRINE T SUPPRESSOR FACTOR FROM MURINE LEUKEMIA
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作者 王维新 吴克复 应红光 《Chinese Journal of Cancer Research》 SCIE CAS CSCD 1991年第2期4-7,共4页
The leukemia-associated autoinhibitor (LAI-615) derived from murine leukemia L7811 has been investigated intensively in our laboratory. In the following experiments, the partial purification of LA I-615 has been carri... The leukemia-associated autoinhibitor (LAI-615) derived from murine leukemia L7811 has been investigated intensively in our laboratory. In the following experiments, the partial purification of LA I-615 has been carried out in addition to the observation of phenotype variations of L7811 leuke-mic cells. The factor was purified over 1306-fold by sequential fractionation with Sephadex G-150 gel filtration, DEAE-cellulose ion exchange chromato-graphy, and Mono Q-fast protein liquid chromato-graphy. The molecular weight of LAI-615 was 68,000 as estimated by gel filtration. LAI-615 was a protein but not glycosylated, and it was suggested LAI-615 be secreted in an autocrine manner. Im-munocytochemical staining showed that the expression of Lyt2 phenotype of L7811 leukemic cells was often coincident with the secretion of LAI-615. Moreover, the physicochemical characteristics of LAI-615 was similar to that of T suppressor factor. Thus it is concluded that LAI-615 may be one of TsF-like factors. 展开更多
关键词 LAI PARTIAL purification AND CHARACTERIZATION OF AN AUTOCRINE T SUPPRESSOR factor FROM MURINE LEUKEMIA DEAE FPLC
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