An avian serum alpha 1-glycoprotein, hemopexin, differing significantly in both amino acid and carbohydrate composition from mammalian (beta-glycoprotein) counterparts.

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 and particularly in lysine, has a much higher glutamine/glutamate and arginine content, and also a higher proline, glycine, and histidine content, than the mammalian hemopexins. Compositional analyses and 125I concanavalin A and 125I wheat germ agglutinin binding suggest that chicken hemopexin has a mixture of three fucose-free N-linked bi- and triantennary oligosaccharides. In contrast, human hemopexin has five N-linked oligosaccharides and an additional O-linked glycan blocking the N-terminal threonine residue [Takahashi, N., Takahashi, Y., & Putnam, F. W. (1984) Proc. Natl. Acad. Sci. U.S.A. 81, 2021-2025], while the rabbit form has four N-linked oligosaccharides [Morgan, W. T., & Smith, A. (1984) J. Biol. Chem. 259, 12001-12006]. In keeping with the finding of a simpler carbohydrate structure, the avian hemopexin exhibits only a single band on polyacrylamide gel electrophoresis under both nondenaturing and denaturing conditions, whereas the hemopexins of the three mammalian species tested show several bands.(ABSTRACT TRUNCATED AT 250 WORDS)

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