Hucolin, a new corticosteroid‐binding protein from human plasma with structural similarities to ficolins, transforming growth factor‐β1‐binding proteins

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Abstract
In order to study the cortisol-binding factors in blood, human plasma was applied to a 11β-hydroxy-3-oxo-4-androstene-17β-carboxyaminoethylamine-(HACA) 1,4-butanediol diglycidyl ether-Sepharose column. Elution of the column with cortisol buffer produced two protein peaks, the minor peak yielded a protein complex of molecular weight ∼200 kDa, subsequently termed hucolin. SDS-PAGE analysis under reducing and non-reducing conditions revealed hucolin was a disulphide-linked complex of 35-kDa and 75-kDa subunits. Twenty-five amino acid residues of the N-terminus of the 35-kDa subunit were determined and homology searches revealed an 88% sequence identity with the N-terminal region of β-ficolin, a transforming growth factor-β1 (TGF-β1)-binding protein purified from porcine uterus