Isolation and properties of carboxylesterase from hemolymph of the silkworm Bombyx mori L

Naletova, E.A.; Egorova, T.A.; Filippovich, I.B.

Biokhimiia 47(11): 1844-1851


ISSN/ISBN: 0320-9725
PMID: 6185156
Accession: 005766133

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An original procedure for isolation and purification of carboxylesterase from the hemolymph of stage V larvae of a B. mori strain, including precipitation with 10% polyethyleneglycol, ion-exchange chromatography on Sephadex G-200 and chromatography, was developed. Some physicochemical properties of the enzyme (MW = 69,000, pI .simeq. 4.9, temperature optimum = C, pH optimum = 7.2, Km for .alpha.-naphthyl- and .beta.-naphthylacetate = 0.11 .cntdot. 10-3 and 0.52 .cntdot. 10-3 M, respectively) were determined. Using immunodiffusion in agar gel, the antigenic identity of the enzymes isolated from the hemolymph of 2 silkworm species was established.