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. 1998 Mar 27;244(3):796-800.
doi: 10.1006/bbrc.1998.8344.

Molecular cloning and characterization of mouse ficolin-A

Y Fujimori  1 , S Harumiya, Y Fukumoto, Y Miura, K Yagasaki, H Tachikawa, D Fujimoto
Affiliations

Molecular cloning and characterization of mouse ficolin-A

Y Fujimori et al. Biochem Biophys Res Commun. .

Abstract

A novel ficolin-related gene was isolated from the mouse liver lambda ZAPII cDNA library. The protein encoded by this gene consists of both collagen- and fibrinogen-like domains, which are common features of the ficolin family, and was named mouse ficolin-A. The amino acid sequence of mouse ficolin-A is 60.2, 59.8, 59.8, and 59.6% identical to those of porcine ficolin-alpha, -beta, human ficolin-1, and EBP-37/P35, respectively. Northern blot analysis showed that mRNA of mouse ficolin-A is highly expressed in liver and spleen. Immunoblot analysis using an anti-mouse ficolin-A antiserum showed that mouse ficolin-A is a plasma protein with binding activity to elastin and GlcNAc.

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