Studies on the integument of cestodes. II. The nature of protein component in the integument of gravid proglottides of Taenia hydatigena.
The main cuticle of the gravid proglottides shows differences in their chemical make up, in that there is a transformation of SH groups into -S-S bonding resulting in the refractivity of the cuticle. Another feature is the coexistence of dityrosine linkages with -S-S bondings. The mode of dityrosine formation from tyrosine residues is found to be possible by the presence of a peroxidase enzyme system in the cuticle. The evolutionary and physiological significance of the occurrence of -S-S bonding and dityrosine links have been discussed.
D000818:Animals; D001665:Binding Sites; D004220:Disulfides / Q000032:analysis; D005260:Female; D010544:Peroxidases / Q000032:analysis; D010636:Phenols / Q000032:analysis; D011487:Protein Conformation; D011506:Proteins / Q000032:analysis*; D012098:Reproduction; D012867:Skin / Q000032:analysis*; D013194:Staining and Labeling; D013438:Sulfhydryl Compounds / Q000032:analysis; D013621:Taenia / Q000033:anatomy & histology / Q000502:physiology*; D014443:Tyrosine / Q000032:analysis
D004220:Disulfides; D010636:Phenols; D011506:Proteins; D013438:Sulfhydryl Compounds; D014443:Tyrosine; D010544:Peroxidases