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pubmed:abstractText |
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 alpha 2HS glycoprotein. The N-terminal 105 residues and a segment aligned with residues 170-225 of alpha 2HS 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 alpha 2HS.
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