Esterase patterns in human saliva established by chromatography on Con-A-Sepharose and by isoelectric focusing

Abstract

The heterogeneity of esterases from human whole saliva was studied by gel chromatography, isoelectric focusing and affinoelectrophoresis. Concanavalin A (Con A) and lentil leetin bound to an esterase with a pI value of 5, whereas an esterase with a pI value of 6 interacted only with Con A. Both esterases appeared as several different charged forms after isoelectric focusing on acrylamide gels and had molecular weights of 28,000 (pI = 5) and 45,000 (pI = 6). A third esterase, molecular weight 7000, was distinguished from the other esterases by inability to hydrolyse naphthyl esters or bind to lectins.