Journal article

AN AVIAN SERUM ALPHA-1-GLYCOPROTEIN, HEMOPEXIN, DIFFERING SIGNIFICANTLY IN BOTH AMINO-ACID AND CARBOHYDRATE-COMPOSITION FROM MAMMALIAN (BETA-GLYCOPROTEIN) COUNTERPARTS

V GOLDFARB, RB TRIMBLE, M DEFALCO, HH LIEM, SA METCALFE, D WELLNER, U MULLEREBERHARD

BIOCHEMISTRY | AMER CHEMICAL SOC | Published : 1986

Abstract

We report here on physicochemical characteristics of chicken hemopexin, which can be isolated by heme-agarose affinity chromatography [Tsutsui, K., & Mueller, G. C. (1982) J. Biol. Chem. 257, 3925-3931], in comparison with representative mammalian hemopexins of rat, rabbit, and human. The avian polypeptide chain appears to be slightly longer (52 kDa) than the human, rat, or rabbit forms (49 kDa), and also the glycoprotein differs from the mammalian hemopexins in being an alpha 1-glycoprotein instead of a beta 1-glycoprotein. This distinct electrophoretic mobility probably arises from significant differences in the amino acid composition of the chicken form, which, although lower in serine an..

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