Trace proteins in cerebrospinal fluid and other biological fluids: II. Effect of storage and enzymes on the electrophoretic mobility of γ- trace and β-trace proteins in cerebrospinal fluid

Abstract

Storage of concentrated human CSF at −10° for about one week leads to a shift in the electrophoretic mobility of part of the γ-tr protein towards the anode. This results in a double arc appearance in immunoelectrophoresis. After prolonged storage only the arc of faster mobility is observed. Storage of CSF in unconcentrated form at −10° also induces this change but at a much slower rate. Other temperatures tested were much less effective. Treatment with papain of stored CSF resulted in a reverse shift in mobility of the γ-tr protein and a marked reduction in concentration. The slow mobility product of papain treatment was resistant to the effect of storage at −10°. Neuraminidase treatment of CSF resulted in a slower mobility of β-tr but did not significantly affect the γ-tr protein.