Structure-Function Relationships of Erythropoietin

作者: T. R. J. Lappin

DOI: 10.1007/978-3-642-77074-6_1

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摘要: One of the major questions in erythropoietin research centres on relationship between structure hormone and its mode action. Erythropoietin is a glycoprotein which 39% carbohydrate based molecular mass 30 400 daltons, as determined by sedimentation equilibrium [1]. The human gene encodes 193 amino acid protein. Cleavage 27 leader sequence gives mature protein undergoes post-translational processing. N-linked glycosylation occurs at three asparagine sites, residues 24, 38 83 [2] O-linked serine residue 126 [3] (see Fig. 1). In addition, C-terminal arginine (residue 166) removed, possibly an intracellular carboxypeptidase [4].

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