Abstract
Thyroglobulin fractions rich and poor in new thyroglobulin were separated by means of DEAE-cellulose chromatography of dog thyroid extracts and by zonal ultracentrifugation in a sucrose gradient of guinea pig thyroid extract incubated at low temperature. The distrubtion of thyroxine, triiodothyronine and 3,3',5'-(reverse)-triidothyronine in hydrolysates of the different fractions was estimated by radioimmunoassays. Following DEAE-cellulose chromatography there was a small but statistically significant increase in T4/T3 ratio in thyroglobulin fractions eluted at high ionic strength--that is fractions relatively rich in stable iodine but poor in fresh thyroglobulin. There was no differences in the T4/rT3 ratios between the different fractions. The ratios between iodothyronines were almost identical in the various thyroglobulin fractions following zonal ultracentrifugation in a sucrose gradient of cold treated guinea pig thyroid extract. These findings lend no support to the possibility that a relatively high content of triiodothyronines in freshly synthesized thyroglobulin modulates the thyroid secretion towards a preferential secretion of triiodothyronine and 3,3',5'-(reverse)-triidothyronine at the expense of the secretion of thyroxine.
Original language | English |
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Journal | Acta endocrinologica |
Volume | 88 |
Issue number | 2 |
Pages (from-to) | 298-305 |
Number of pages | 8 |
ISSN | 0001-5598 |
Publication status | Published - Jun 1978 |
Externally published | Yes |
Keywords
- Animals
- Centrifugation, Zonal
- Chromatography, DEAE-Cellulose
- Dogs
- Guinea Pigs
- Radioimmunoassay
- Thyroglobulin
- Thyroid Gland
- Thyroxine
- Triiodothyronine