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R Pitt-Rivers

Publications and source records attributed to R Pitt-Rivers.

14 recordsLinked to original sources
PubMed1976

The subunit structure of thyroglobulin.

Human and rat thyroglobulin were reduced and alkylated in aqueous alkaline conditions in the absence of denaturants; the product of reduction in both cases has been found to have mol.wt. about 165000, or one-quarter that of the native molecule.

Alkylation↗
PubMed1970

The subunits of thyroglobulin.

1. Pig thyroglobulin was reduced with dithiothreitol in the presence of sodium dodecyl sulphate, 8m-urea or 6m-guanidinium chloride. 2. The molecular weights of the reduction products were about 165000. 3. Two stable subunits with molecular weights as low as 35000 and 20000 were separated by Sephadex chromatography after prolonged exposure of the reduction products to sodium dodecyl sulphate at pH8.7. Although a hydrolytic reaction is probably implicated, the nature of the chemical linkages broken was not established.

Animals↗
PubMed1970

Radioautographic studies of the initial site of formation of protein-bound iodine in the rat thyroid gland.

1. Predominantly cellular labelling was observed in radioautographs of rat thyroid glands fixed by perfusion from the aorta at intervals between 5 and 55s after [(125)I]iodide administration via the aorta. 2. When perfusion was delayed for 2min, or if immersion fixation was used, the labelling was predominantly over the peripheral portion of the follicular lumen, in agreement with the observations of other investigators. 3. The findings support the concept that the initial site of binding of iodine to protein is intracellular, but the nature of this protein has not been established.

Animals↗
PubMed1968

The binding of sodium dodecyl sulphate to various proteins.

1. The binding of sodium dodecyl sulphate to proteins by equilibrium dialysis was investigated. 2. Most of the proteins studied bound 90-100% of their weight of sodium dodecyl sulphate. 3. The glycoproteins studied bound 70-100% of their weight of sodium dodecyl sulphate, calculated in terms of the polypeptide moiety of the molecule. 4. Proteins not containing S.S groups bound about 140% of their weight of sodium dodecyl sulphate. 5. Reduction of four proteins containing S.S groups caused a rise in sodium dodecyl sulphate binding to 140% of the weight of protein. 6. The apparent micellar molecular weights of the protein-sodium dodecyl sulphate complexes were measured by the dye-solubilization method; they were all found to have approximately the same micellar molecular weight (34000-41000) irrespective of the molecular weight of the protein to which they were attached.

Catalase↗