A new method of coupling proteins to insoluble polymers |
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Authors: | P V Sundaram |
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Affiliation: | Department of Physiology, Thrombosis Specialized Center of Research, Wayne State University School of Medicine, Detroit, Michigan 48201 USA |
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Abstract: | The A chain isolated from biologically active human thrombin is thirteen residues shorter from the amino terminus than the A chain isolated from bovine thrombin. Automated Edman degradation of the reduced, alkylated A chain permitted the direct identification of 34 out of the 36 residues and established all tryptic overlaps. The NH2-terminal residue is threonine. This residue is homologous to threonine-14 of the A chain of bovine thrombin. Human thrombin A chain has one half cystine linking it to the larger B chain. Methionine, histidine, valine and tryptophan are not present. There are nine acid residues (Glu, Asp) but none of their respective amides. |
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