Isolation and purification of plasma albumin from human blood samples

Abstract

This study isolated plasma albumin from human blood samples using cold 19% v/v ethanol as well as containing 0.6 % v/v trichloro acetic acid for the isolation of albumin from blood serum or plasma using organic solvents after standing for 5hr. The precipitated plasma albumin was then fractionated using 90% ethanol containing 0.14% hydrochloric and was finally neutralized with 0.5 mol.dm-3 NaOH to obtain a white flocculent precipitate of plasma albumin which was dried over P 2 O 5 to obtain a percentage recovery of 1.36 %. The dried isolated plasma albumin was further characterized for purity using protein analysis, optical rotation , solubility and denaturation tests. The results show the plasma album contained 63.67% protein , with specific rotation at[α] 598 32 at pH 7.2 of 8 0 and gradually dissolved in acidified water and ethanol. The plasma albumin was also found to be slightly turbid when dissolved in water indicating some degree of denaturation.