In-vitro stability of human alpha-fetoprotein.

We assessed the stability of alpha-fetoprotein (AFP) in clinical specimens in the presence and absence of serum and albumin, at different temperatures and concentrations. We find it depends on both AFP concentration and incubation temperature. Dilution of most specimens with either phosphate buffer or phosphate-buffered saline or by immunoelectrodiffusion resulted in some loss of AFP. Attempts to stabilize AFP during either sample dilution or incubation by use of albumin in concentrations up to 1 g/L did not protect it from inactivation unless normal human serum was also included. Frozen AFP solutions were less stable than solutions stored at 4 degrees C. AFP was most stable when lyophilized and stored desiccated. The AFP-inactivation curves were usually nonlinear. Apparently both polymerization and degradation occur simultaneously as AFP loses its activity. Proteolytic enzyme inhibitor and sulfhydryl reagent not only failed to protect it from inactivation, they appeared to speed it.