| Abstract: | An original procedure for isolation and purification of carboxylesterase from the hemolymph of stage V larvae of one of Bombyx mori strains including precipitation with 10% polyethyleneglycol, ion-exchange chromatography on Sephadex G-200 and chromatography on DEAE-Sephadex A-50, has been developed. The specific activity of the enzyme after purification makes up to 1250 units per mg of protein with a 59% yield. Some physicochemical properties of the enzyme (Mr = 69 000, pI congruent to 4.9, temperature optimum = 40 degrees, pH optimum = 7.2 Km for alpha-naphthyl- and beta-naphthylacetate = 0.11 X 10(-3) and 0.52 X 10(-3) M, respectively) have been determined. Using immunodiffusion in agar gel, the antigenic identity of the enzymes isolated from the hemolymph of two silkworm species has been established. |
