par Brachet, Jean 
;Jeener, Raymond
Référence Biochimica et biophysica acta, 1, C, page (13-20)
Publication Publié, 1947
;Jeener, Raymond Référence Biochimica et biophysica acta, 1, C, page (13-20)
Publication Publié, 1947
Article révisé par les pairs
| Résumé : | 1. 1. The physical and chemical properties of both Szent-Györgyi's structure proteins and thymonucleohistone are very much alike; renosine contains more than 2% thymonucleic acid. 2. 2. When cells are treated with Edsall-urea solution and crushed, the nuclei may elongate into birefringent fibers of thymonucleohistone. 3. 3. The viscosity and flow birefringence of renosine show a swift and sharp decrease when thymonucleo-depolymerase is added to the protein. 4. 4. Anucleated cells or cells provided with a very small nucleus fail to give any appreciable amount of structure proteins. 5. 5. The conclusion is drawn that structure proteins are a mixture of cytoplasmic and nuclear components, their specific physical properties being due to a nuclear constitruent, thymonucleoshitone. thymonucleohistone. 6. 6. The relationship between structure proteins, thymonucleohistone, Bensley's plasmosine and the anisometric proteins of the Amphibian neurula (Lawrence, Needham and Shen) is briefly discussed. |
