Purification and characterization of the stage-specific embryonic enhancer-binding protein SSAP-1.
نویسندگان
چکیده
منابع مشابه
The embryonic enhancer-binding protein SSAP contains a novel DNA-binding domain which has homology to several RNA-binding proteins.
Stage-specific activator protein (SSAP) is a 43-kDa polypeptide that binds to an enhancer element of the sea urchin late histone H1 gene. This enhancer element mediates the transcriptional activation of the late histone H1 gene in a temporally specific manner at the mid-blastula stage of embryogenesis. We have cloned cDNAs encoding SSAP by using polyclonal antibodies raised against purified SSA...
متن کاملNew B-lymphocyte-specific enhancer-binding protein.
We report the discovery of a new B-lymphocyte-specific enhancer-binding protein. A series of gel retardation assays using fragments that scan the -2172 to -1180 region of the major histocompatibility complex class II gene E alpha reveal a site (W) that serves as the recognition sequence for two nuclear proteins, one B-cell restricted and the other ubiquitously occurring. Certain characteristics...
متن کاملThe beta-globin stage selector element factor is erythroid-specific promoter/enhancer binding protein NF-E4.
The analysis of transcriptional regulatory proteins is often hampered because such factors are present in cells in only sparing abundance. Although direct biochemical purification has been successfully applied to the analysis of many of these factors, such methods are labor intensive and expensive. We have developed an alternative strategy to identify and characterize such trans-acting factors ...
متن کاملPurification and characterization of antiviral protein from silkworm fecal matter
Antiviral proteins (AVP), present in silkworm fecal matter, show activity against nuclear polyhedrosis virus (NPV) in vitro and in vivo. The extract of silkworm fecal matter prepared in phosphate buffer solution of pH 7.5 was subjected to 50% solid ammonium sulfate precipitation to enrich AVP, then which was dialyzed. The dialysate was applied to the column containing silica gel-G, the column e...
متن کاملPurification and characterization of mouse serum protein with specific binding affinity for C4 (Ss protein)
A new component of the complement (C).system, with a specific binding affinity for the activated Ss-protein (C4) has been identified in mouse serum. This protein, named Ss- (or C4)-binding protein (Ss-bp), was purified about 200 times from mouse plasma. Ss-bp is a heat stable (56 degrees C, 60 rain) beta-globulin with a sedimentation coefficient in sucrose density ultracentrifugation of 10s. It...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Molecular and Cellular Biology
سال: 1993
ISSN: 0270-7306,1098-5549
DOI: 10.1128/mcb.13.3.1746