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- W2000900462 abstract "Two JH carboxylesterases were isolated from haemolymph of vitellogenic females by anion exchange chromatography. The high degree of purification achieved by this one step procedure is inferred by the absence of any protein stainable band (Coomassie blue or silver stain) on native polyacrylamide gels, yet enzyme activity was detectable in eluates of these gels. Purified JH esterases were stable for more than eight months when stored at 5°C. Freezing at −25°C destroyed their activity. Both enzymes lost their activity upon heating to 65°C. The average apparent molecular weights of these esterases were 52,000 and 42,000. The corresponding average Kms of the purified enzymes were approx. 0.68 × 10−6 and 1.54 × 10−6 M. In the haemolymph of newly emerged, allatectomized, and pregnant females only one esterase (mol. wt 52,000) was identifiable. The second esterase was, however, inducible in allactectomized females by the JH analogue methoprene (ZR-515). In all cases, purification by ion exchange chromatography resulted in an approx. 1000-fold gain in JH esterase activity. The removal of several esterase inhibitors accounts for this gain. Neither of the two identifiable JH esterases degraded α-naphthyl acetate (α-NA). A population of esterases which effectively degraded α-NA but did not hydrolyze JH-III eluted from the QAE column before the JH esterases." @default.
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- W2000900462 date "1984-01-01" @default.
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- W2000900462 title "Esterolytic degradation of juvenile hormone in the haemolymph of the adult female of Leucophaea maderae" @default.
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- W2000900462 doi "https://doi.org/10.1016/0020-1790(84)90017-9" @default.
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