CHARACTERIZATION OF N-TERMINAL AMINO-ACID-SEQUENCE OF MONOCLONAL NONSPECIFIC SUPPRESSOR FACTOR

被引：8
|
作者：
NAKAMURA, M [1 ]
OGAWA, H [1 ]
TSUNEMATSU, T [1 ]
机构：
[1] WAKAYAMA RED CROSS HOSP, DIV INTERNAL MED 3, WAKAYAMA 640, JAPAN
来源：
CELLULAR IMMUNOLOGY | 1992年 / 139卷 / 01期
关键词：
D O I：
10.1016/0008-8749(92)90107-Z
中图分类号：
Q2 [细胞生物学];
学科分类号：
071009 ; 090102 ;
摘要：
Monoclonal nonspecific suppressor factor (MNSF), a product of a murine T cell hybridoma, suppresses the antibody response to lipopolysaccharide. In an attempt to clarify the N-terminal sequence, MNSF was prepared and purified by affinity chromatography with the use of an anti-MNSF monoclonal antibody (MO6), and reverse-phase high-pressure liquid chromatography. On the SDS-PAGE, the purified MNSF showed a single band with a molecular weight of 12,000. The N-terminal amino acid sequence of the protein was determined and showed no strong homology to any of the sequences of known biologically active proteins. However, the sequence revealed significant (60%) amino acid identity to transforming growth factor β2 (TGFβ2). © 1992.
引用
收藏
页码：139 / 144
页数：6
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