9 S thyroid particulate iodoprotein.

Particulate iodoproteins have been studied in the rat thyroid gland using the isotopic 125I equilibration method. Pulse experiments were also performed with a second isotope, 131I. Labelled iodoproteins, both soluble and solubilized by digitonin from the thyroid particulate material, were analyzed by sucrose-gradient ultracentrifugation. 1. At isotopic equilibrium and irrespective of the iodide content of the diet two particulate iodoproteins, with sedimentation coefficients of 27 and 19 S, were solubilized by digitonin. In addition a 9 S iodoprotein was also present but its proportion varied markedly with the iodine content of the diet: it accounted for 50-60% of the label found at the particulate level when the dialy diet of iodine was high (75-500 mug/day) but was almost absent when the diet was only 2 mug/day. 2. Most of this 9 S protein was found in the 600-15 000 times g particulate pellet, i.e. a fraction enriched in lysosomes and phagolysosomes. 3. The iodoamino acid composition of the 9 S fraction was very similar to that of the 19 S particulate thyroglobulin: its hormone content was 19%. 4. The double precipitation technique showed that the 9 S fraction is immunochemically related to thyroglobulin. 5. Pulse experiments showed that the 9 S particulate iodoprotein was slowly labelled by 131I. 6. The amount of 9 S iodoprotein was increased by thyrotropin (30-40% increase versus control experiments 5 min after thyrotropin injection). These properties of the 9 S particulate iodoprotein are discussed in relation to the assumption that it might be a product of partial proteolysis of thyroglobulin after endocytosis and partial digestion by the phagolysosomes.     

Subunit structure of 27 S thyroid iodoprotein.

The dissociation of thyroid 27 S iodoprotein by sodium dodecyl sulfate (SDS) and by succinic anhydride was investigated by means of ultracentrifugation and polyacrylamide gel electrophoresis. The iodoprotein obtained from either a human or hog was dissociated into three kinds of subunits (S-19, S-17 and S-12) by SDS treatment. At increased concentrations of SDS, the S-12 subunit was predominant among the dissociation products. The succinylation of 27 S iodoprotein showed essentially the same dissociation pattern as in the case of SDS treatment. This dissociation products of the protein preparations of different animals were qualitatively the same as those of thyroglobulin of the respective animals, confirming the hypothesis that 27 S iodoprotein was composed of two molecules of thyroglobulin. However, the extent of dissociation of 27 S iodoprotein measured by S-12 formation showed higher resistancy of the protein to the dissociating agents than that of thyroglobulin. The contents of sialic acid and hexose as well as iodoamino acids of 27 S iodoprotein were found to be the same as, or not far from, those of thyroglobulin; The dissociability and chemical composition of 27 S iodoprotein was discussed with reference to the subunit structure of the protein.     

The effect of iodide administration on hog thyroid gland and the composition of thyroglobulin and 27-S iodoprotein.

The effect of excess iodide on hog thyroid gland has been examined with regard to the change in the chemical composition of thyroglobulin and in the accumulation of 27-S iodoprotein by the in vivo treatment of hogs with iodide for various lengths of time. The iodine content of thyroglobulin was either unchanged by short term administration of excess iodide, or somewhat lowered. However, the iodine content as well as the total amount of thyroglobulin increased in the glands enlarged by prolonged treatment with iodide. The iodine highest reached 1.17% of the protein on an average. On the other hand, 27-S iodoprotein decreased and finally disappeared after the chronic treatment. Monoiodotyrosine and diiodotyrosine increased in parallel with the increase in the iodine content (0.15 to 1.17%) caused by the iodide treatment, while thyroxine increased but reached a plateau at the level of three residues per mole of thyroglobulin, and no change was observed even in the proteins with the higher iodine content than 0.75%. Proteolytic activity measured by amino acid release from the thyroid protein was depressed by the chronic treatment. On the other hand, the amount of iodocompound released by the autoproteolysis, which may reflect hormone secretion, increased, possibly because of the marked increase in the iodine content of thyroglobulin.     

The blood and lymph bed in Haversian bone

The structure of the components of the Haversian canals of the osseous tissue of the adult human mandible was studied in celloidin sections stained with haematoxylin and eosin. Fine blood vessels - mostly profiles of postcapillary venules, precapillaries and occasional capillaries - were demonstrated in osteons with Haversian canals 60-80 microns in diameter. Neither lymph capillaries nor vessels were observed, even in wider Haversian canals with larger blood vessels. The intraosseal spaces with rich blood vessel plexuses likewise did not contain any lymphatics with a characteristic form.