[Isolation and properties of carboxylesterase from hemolymph of the silkworm Bombyx mori L].
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.
D000818:Animals; D012831:Bombyx / Q000201:enzymology*; D002265:Carboxylic Ester Hydrolases / Q000302:isolation & purification* / Q000378:metabolism; D000939:Epitopes / Q000032:analysis; D006458:Hemolymph / Q000201:enzymology*; D005779:Immunodiffusion; D007700:Kinetics; D008970:Molecular Weight; D013045:Species Specificity; D013696:Temperature
D000939:Epitopes; D002265:Carboxylic Ester Hydrolases
Vydelenie i svoĭstva karboksilesterazy iz gemolimfy tutovogo shelkopriada Bombyx mori L.