Detection of arginine esterase activity in human follicular fluid

Abstract

One major fraction hydrolysing arginine ester and amido derivative (major preparation) was detected and separated from human follicular fluid by Cellulofine GCL-2000 gel filtration. The best ester and amide substrates for this preparation were acetyl-glycyl-lysine methyl ester (Ac-Gly-Lys-Me) and D-valyl-L-leucyl-L-arginine-p-nitroanilide (Val-Leu-Arg-pNA), respectively. The preparation contained plasmin and plasminogen; lysine-Cellulofine adsorption and elution changed the substrate specificity of its esterolytic activity. After treatment by lysine-Cellulofine adsorption and elution, the basic and acidic arginine esterase activities of the major preparation were separated by CM- and DEAE-cellulose adsorption and elution, respectively. The substrate specificity of these two esterolytic enzyme activities differed before and after adsorption of the major preparation to the lysine affinity column.