EBP-37, A NEW ELASTIN BINDING-PROTEIN IN HUMAN PLASMA - STRUCTURAL SIMILARITY TO FICOLINS, TRANSFORMING GROWTH-FACTOR-BETA-1 BINDING-PROTEINS

In order to study the elastin-binding factors in blood, human plasma w as applied to an alpha-elastin-Sepharose column. The column-binding fr action contained a 37-kDa protein, which was tentatively named EBP-37. Partial amino acid sequences of EBP-37 were determined. It had collag enous and non-collagenous domains, Homology searches of the sequences revealed that the protein is very similar but not identical to ficolin s, transforming growth factor-beta 1 (TGF-beta 1)-binding proteins fro m porcine uterus membranes, Direct interaction of EBP-37 with elastin was confirmed by demonstrating the binding of the isolated EBP-37 to a lpha-elastin on a nitrocellulose membrane using the EBP-37-specific an tiserum, The existence of oligomers and multimers crosslinked by disul fide bonds was demonstrated by immunoblot analysis, Possible functions of EBP-37 are discussed.