[RNA-binding proteins of Rana temporaria frog oocytes. Isolation by methods of affinity chromatography and radioactive labelling in vitro].
A fraction of RNA-binding proteins from the maturating frog oocytes of Rana temporaria was isolated by the method of affinity chromatography on poly-U coupled to Sepharose. These proteins were labelled with high activity by the method of reductive methylation using 3H-sodium borohydride. It was shown that during the isolation and labelling there is no loss or inactivation of any RNA-binding protein fraction which is essential for informosome-like particles formation. The molecular masses of polypeptide chains in the isolated RNA-binding protein fraction were determined.
D000818:Animals; D001001:Anura; D002250:Carbon Radioisotopes; D002352:Carrier Proteins / Q000302:isolation & purification*; D002846:Chromatography, Affinity / Q000379:methods; D004527:Egg Proteins / Q000302:isolation & purification*; D005260:Female; D007553:Isotope Labeling / Q000379:methods; D008970:Molecular Weight; D009865:Oocytes / Q000032:analysis*; D010063:Ovum / Q000032:analysis*; D010455:Peptides; D012313:RNA; D011896:Rana temporaria
D002250:Carbon Radioisotopes; D002352:Carrier Proteins; D004527:Egg Proteins; D010455:Peptides; D012313:RNA
RNK-cviazyvaiushchie belki ootsitov liagushki Rana temporiria. Vydelenie metodom affinnoĭ zhromatografii i radioaktivnoe mechenie in vitro.