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Fetuin: The bovine homologue of human α 2 HS glycoprotein
Author(s) -
Christie D.L.,
Dziegielewska K.M.,
Hill R.M.,
Saunders N.R.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80010-8
Subject(s) - fetuin , polyclonal antibodies , glycoprotein , trypsin , antibody , microbiology and biotechnology , biochemistry , peptide sequence , chemistry , in vitro , biology , genetics , enzyme , gene
The fetal protein fetuin has previously been considered to be confined to species of the order Artiodactyla (cattle, sheep, etc.) in spite of demonstrable biological in vitro effects in tissues of other species [(1983) Comp. Biochem. Physiol. 76A, 241–245]. We have determined the partial amino acid sequence of bovine fetuin and compared it with the published sequence of human α 2 HS glycoprotein. The N‐terminal 105 residues and a segment aligned with residues 170–225 of α 2 HS glycoprotein revealed 109 of 161 residues to be identical between the two proteins (68% homology). Mouse polyclonal antibodies to fetuin, and trypsin digest fragments of this protein have been prepared and used for a comparison of native and digested proteins. Polyclonal antibodies to native protein showed little if any cross reactivity. However, antibodies to trypsin digest fragments of fetuin showed obvious cross reactivity with α 2 HS.