Subcellular structure of bovine thyroid gland. The localization of the peroxidase activity in bovine thyroid.

  title={Subcellular structure of bovine thyroid gland. The localization of the peroxidase activity in bovine thyroid.},
  author={M. D. De Wolf and A. Lagrou and H. Hilderson},
  journal={The Biochemical journal},
  volume={174 3},
1. After differential pelleting of bovine thyroid tissue the highest relative specific activities for plasma membrane markers are found in the L fraction whereas those for peroxidase activities (p-phenylenediamine, guaiacol and 3,3'-diaminobenizidine tetrachloride peroxidases) are found in the M fraction. 2. When M + L fractions were subjected to buoyant-density equilibration in a HS zonal rotor all peroxidases show different profiles. The guaiacol peroxidase activity always follows the… Expand
13 Citations
Peroxidase, an alternate pathway to cytochrome P-450 for xenobiotic metabolism in skin: partial purification and properties of the enzyme from neonatal rat skin.
Subcellular distribution studies indicated the activity to be highest and comparable in nuclei and mitochondria, lowest in microsomes, and absent in cytosol, while the combination of 2 mM N-ethylmaleimide and 10% (w/v) glycerol was found to be optimal for preservation of activity. Expand
The subcellular biochemistry of thyroid.
Conditions and results of differential pelleting and gradient centrifugation studies are described with special attention to the validity of the markets used and enriched subcellular fractions have been isolated which have been useful for biochemical studies concerning the specific function of this tissue. Expand
Peroxidase: a novel pathway for chemical oxidation in human term placenta.
The results suggest that peroxidase may be a major enzyme in human term placenta capable of oxidation of endogenous chemicals and xenobiotics. Expand
Characterization of thyroid follicular cell apical plasma membrane peroxidase using monoclonal antibody.
Thyroid peroxidase (TPO) located in the apical plasma membrane of follicular cells was investigated by means of a membrane-immunofluorescent technique and it was thought that TPO reappearance is mediated by other than the adenylate cyclase-cyclic AMP system. Expand
On the binding of dolichol by bovine liver supernatant.
Experimental evidence is presented that a bovine liver pH 5.1 supernatant possesses binding capacity towards dolichol, and the involvement of a protein-like structure is inferred from ammonium sulphate precipitation and proteolysis experiments. Expand
Characterization of the in vitro conversion of dolichol to dolichoate in bovine thyroid.
Investigation of cofactor requirements revealed that NAD+ was essential for reaching optimal activity in the enzymic conversion of dolichol into dolichoic acid, and inhibitor studies showed the conversion system behaves distinctly differently from the NADP(+)-depending microsomal oxidoreductase as well as from catalase. Expand
Occurrence and subcellular localization of glucose 6-phosphatase in bovine thyroid.
In bovine thyroid tissue the glucose 6-phosphatase activity is not entirely due to the presence of an unspecific acid phenylph phosphatase, but it can be used as a marker for endoplasmic reticulum membranes after centrifugation in a zonal rotor. Expand
Detection of a catalytic intermediate of peroxidase in hog thyroid microsomes.
It was concluded that thyroid peroxidase exhibits the same peroxIDase activity for guaiacol or ascorbate in the free and the microsome-bound forms. Expand
Topography, purification and characterization of thyroidal 5'-nucleotidase.
Thyroidal 5'-nucleotidase can be classified as an unspecific metallo-dependent 5'-ribonucleotide phosphohydrolase, which exists as a dimer composed of two similar or identical subunits. Expand
Biosynthesis of thyroid hormones.
  • R. Ekholm
  • Biology, Medicine
  • International review of cytology
  • 1990
The chapter reviews the mechanisms for iodination and coupling and the iodide transport, the characteristics of thyroperoxidase, the generation of hydrogen peroxide, and thyroglobulin chemistry and structure and describes some aspects of the unique morphology of the thyroid. Expand