Abstract
This study included isolation and purification of copepin hormone from heart disease patients serum using different biochemical techniques. The study showed two proteinous peak has been isolated by gel filtration (Sephadex G-50) from the precipitation by cold acetone, the results predicted that (peak B) has a high concentration of copepin . Furthermore, the purity of the isolated copeptin ( peak B) had been identified by SDS-poly acryl amide gel electrophoresis and the reverse phase high performance liquid chromatography in which results showed agood identity in retention time between the standard and the isolated copeptin (peak B) .
 The approximate molecular weight of partially purified copeptin peak (B) was (4654±400 Dalton , ±4513400 Dalton) using gel filtration chromatography (Sephadex G-50) and (SDS-poly acryl amide gel electrophoresis) technique respectively .
 The study of secondary structure (α-helix) to copeptin hormone by the (Circular Dichroesim) showed the percentage of the (α-helix) between the standard solution of copeptin and sample solution (peak B) was good match.
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