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Separation of albumin from autologous plasma by heat
Author(s) -
ZHOW Y.,
ZHU M.,
CHENG J.,
YIAN B.,
YIANG Y.
Publication year - 1992
Publication title -
transfusion
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.045
H-Index - 132
eISSN - 1537-2995
pISSN - 0041-1132
DOI - 10.1046/j.1537-2995.1992.32492263450.x
Subject(s) - albumin , chromatography , chemistry , oncotic pressure , radial immunodiffusion , apheresis , polyacrylamide gel electrophoresis , blood proteins , electrophoresis , immunodiffusion , antibody , immunology , medicine , biochemistry , platelet , enzyme
A simplified technique has been developed to separate albumin from the plasma of a patient undergoing treatment with plasma exchange. This albumin can be returned to the patient to maintain colloid osmotic pressure without risk of transmitting disease. Patient plasma is obtained by apheresis. It is heated at 70 degrees C for 60 minutes to denature and remove autoantibodies, immune complexes, and abnormal globulins. The resulting low‐concentration albumin solution (LCAS) retains its natural properties. Immunologic analysis by gel diffusion shows a reaction pattern of complete identity with that of human serum albumin. The albumin in LCAS is more than 90 percent of the remaining protein, as determined by scan of a cellulose acetate electrophoresis pattern. More than 97 percent of the albumin is in monomer form, as judged by polyacrylamide gel electrophoresis. No patient antibodies to neonantigens in the heat‐treated albumin can be identified by double radial immunodiffusion. More than 80 percent of the plasma albumin is recovered in LCAS. LCAS is safe and efficient for use in plasma exchange.