1995 年 117 巻 5 号 p. 1029-1035
In order to study the elastin-binding factors in blood, human plasma was applied to an α-elastin-Sepharose column. The column-binding fraction contained a 37-kDa protein, which was tentatively named EBP-37. Partial amino acid sequences of EBP-37 were determined. It had collagenous and non-collagenous domains. Homology searches of the sequences revealed that the protein is very similar but not identical to ficolins, transforming growth factor-β1 (TGF-β1)-binding proteins from porcine uterus membranes. Direct interaction of EBP-37 with elastin was confirmed by demonstrating the binding of the isolated EBP-37 to α-elastin on a nitrocellulose membrane using the EBP-37-specific antiserum. The existence of oligomers and multimers crosslinked by disulfide bonds was demonstrated by immunoblot analysis. Possible functions of EBP-37 are discussed.