title: Studies on the integument of cestodes. II. The nature of protein component in the integument of gravid proglottides of Taenia hydatigena.
abstract: 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.
mesh_terms: 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
chemical_list: D004220:Disulfides; D010636:Phenols; D011506:Proteins; D013438:Sulfhydryl Compounds; D014443:Tyrosine; D010544:Peroxidases