RESUMEN

We have isolated, purified and characterized a 42-kDa phosphoprotein which has been found to be preferentially associated with active gene loci of salivary gland cells of Chironomus tentans. The rapidly phosphorylated form of this protein could be extracted with 0.2 M NaCl. Chromatographic analysis by gel filtration revealed that a significant fraction of labelled 42-kDa polypeptide elutes with an apparent molecular mass of 150 to 200 kDa. The result suggests that a portion of the phosphorylated 42-kDa polypeptide in native state forms a multisubunit protein complex consisting of rapidly phosphorylated 42-kDa polypeptide chains alone.

Asunto(s)

Cromosomas/análisis , Proteínas Nucleares/aislamiento & purificación , Fosfoproteínas/aislamiento & purificación , Animales , Chironomidae , Cromatografía en Gel , Sustancias Macromoleculares , Peso Molecular , Proteínas Nucleares/metabolismo , Fosfatos/metabolismo , Fosfoproteínas/biosíntesis , Glándulas Salivales/análisis