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 P2O5 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[á]598 32 at pH 7.2 of 80 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.