Plasma Hyaluronan-binding Protein Is a Serine Protease

Alexander A. Vostrov, Wolfgang W. Quitschke
2000 Journal of Biological Chemistry  
CTCF is an essential factor for optimal transcription from the amyloid ␤-protein precursor promoter. A proteolytic activity detected in bovine, rabbit, horse, and human serum cleaves CTCF at three major sites, resulting in a modified mobility shift pattern of the fragments that retain DNA binding ability. The protease was purified to electrophoretic homogeneity, partially sequenced, and identified as the plasma hyaluronan-binding protein. The proteolytic activity was selectively abolished by
more » ... ely abolished by various serine protease inhibitors, including the Kunitz-type protease inhibitor domain of amyloid ␤-protein precursor. Reduction with ␤-mercaptoethanol showed that the 70-kDa protein consists of two polypeptides with apparent molecular masses of 44 and 30 kDa. The serine protease domain was localized to the 30-kDa polypeptide as determined by [ 3 H]diisopropylfluorophosphate binding.
doi:10.1074/jbc.m904640199 pmid:10816595 fatcat:tgtcgmudq5aibotqa6dvhhfjpu