The egg-shell of Drosophila melanogaster III. Covalent crosslinking of the chorion proteins involves endogenous hydrogen peroxide.

@article{Margaritis1985TheEO,
  title={The egg-shell of Drosophila melanogaster III. Covalent crosslinking of the chorion proteins involves endogenous hydrogen peroxide.},
  author={Lukas H. Margaritis},
  journal={Tissue & cell},
  year={1985},
  volume={17 4},
  pages={553-9}
}
Utilizing two cytochemical methods, namely, diaminobenzidine for the assay of peroxidases and cerium(III) chloride for the localization of hydrogen peroxide it was found that the enzyme exists in two out of the five egg-shell layers: the innermost choronic layer and the endochorion. In addition, hydrogen peroxide which acts as a substrate for the enzyme in vitro enabling the formation of covalent bonding between the egg-shell proteins, was found to be produced at the follicle cell plasma… CONTINUE READING
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