Abstract
Haemolymph of fully grown larvae of Galleria mellonella was chromatographed on Sephadex G-200 and the column eluate assayed for hydrolytic activity and juvenile hormone (JH) binding. Hydrolysis of JH-I and 1-naphthyl acetate (1-NA) by high molecular fractions ( 2 × 10 5 ) was sensitive to 2 × 10 −4 M diisopropylphosphofluoridate (DFP). JH-Hydrolysis by proteins ranging in molecular weight from 1.4 × 10 5 to 3.7 × 10 4 was unaffected by DFP and 2.1 × 10 −4 M p- chloromercuribenzoate (PCMB), whereas the overlapping 1-NA hydrolysis was inhibited by these reagents. Several of the JH-esterase peaks coincided with those which hydrolyzed 4-methylumbelliferyl esters of JH-II acid, JH-III acid and oleic acid. The enzymes hydrolyzing these substrates were also unaffected by DFP and PCMB. Highest non-enzymatic binding of JH occurred in the protein fraction with mol. wt of 2.5 × 10 4 . The binding protected JH against most of the blood esterases.
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