@misc{FerenzPeterBerg1983,
  author    = {Ferenz, Hans-J{\"u}rgen and Peter, Martin G. and Berg, Dieter},
  title     = {Inhibition of farnesoic acid methyltransferase by sinefungin},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus-17016},
  year      = {1983},
  abstract  = {Sinefungin inhibited the S-adenosylmethionine-dependent farnesoic acid methyltransferase in a cell-free system containing a homogenate of corpora allata from female locusts, Locusta migratoria. The enzyme catalyzed the penultimate step of juvenile hormone biosynthesis in the insects. Culturing corpora allata in the presence of sinefungin greatly suppressed juvenile hormone production. The following in vivo effects were visible after injection of the inhibitor: increase in mortality and reduction of total haemolymph protein liter and ovary fresh weight, as well as length of terminal oocytes. Attempts to reverse these effects by topical application of the juvenile hormone analog ZR-515 (methoprene) were only partly successful. Therefore, the in vivo effects may be due to a general inhibition of methyltransferase enzymes in the insect. Sinefungin appeared to be of potential interest as the first representative of a new class of insect growth regulators.},
  language  = {en}
}
@misc{KortPeterKoopmanschap1983,
  author    = {Kort, C. A. D. de and Peter, Martin G. and Koopmanschap, A. B.},
  title     = {Binding and degradation of juvenile hormone III by haemolymph proteins of the Colorado potato beetle: a re-examination},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus-16777},
  year      = {1983},
  abstract  = {The haemolymph of the adult Colorado potato beetle, Lepinotarsa decemlineata Say, contains a high molecular weight (MW > 200,000) JH-III specific binding protein. The Kd value of the protein for racemic JH-III is 1.3 ± 0.2 × 10-7 M. It has a lower affinity for racemic JH-I and it does not bind JH-III-diol or JH-III-acid. The binding protein does discriminate between the enantiomers of synthetic, racemic JH-III as was determined by stereochemical anaysis of the bound and the free JH-III. Incubation of racemic JH-III with crude haemolymph results in preferential formation of (10S)-JH-III-acid, the unnatural configuration. The JH-esterase present in L. decemlineata haemolymph is not enantioselective. It is concluded that the most important function of the binding protein is that of a specific carrier, protecting the natural hormone against degradation by esterases. The carrier does not protect JH-I as efficiently as the lower homologue.},
  language  = {en}
}