PMID: 8586615May 1, 1995Paper

EBP-37, a new elastin-binding protein in human plasma: structural similarity to ficolins, transforming growth factor-beta 1-binding proteins

Journal of Biochemistry
S HarumiyaD Fujimoto

Abstract

In order to study the elastin-binding factors in blood, human plasma was applied to an alpha-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-beta 1 (TGF-beta 1)-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 alpha-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.

Citations

May 30, 1997·The Journal of Biological Chemistry·T Ohashi, H P Erickson
Mar 22, 2002·The Journal of Immunology : Official Journal of the American Association of Immunologists·Misao MatsushitaTeizo Fujita
Nov 23, 2007·Clinical and Experimental Immunology·J FaroH Gewurz
May 16, 2013·Scandinavian Journal of Immunology·S E Degn, S Thiel
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Oct 27, 2009·Molecular Immunology·Michikazu TanioToshiyuki Kohno
Feb 15, 2011·The International Journal of Biochemistry & Cell Biology·Yuichi EndoTeizo Fujita

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