title: Isolation of HnRNP particles from Drosophila melanogaster embryos.
abstract: HnRNP from nitrogen frozen Drosophila melanogaster embryos were isolated in the presence of EDTA and EGTA cosedimenting in sucrose and density gradients like hnRNP from vertebrates. Four "core" proteins of 23.000, 28.000, 32.000 and 45.000 Da are strongly enriched in these complexes. One could conclude that the basic structural organization of Drosophila melanogaster hnRNP is similar to that described for vertebrates.
authors.affiliation: Institut für Molekulare Genetik, Universität Heidelberg, FRG.
authors.forename: J
authors.initials: J
authors.lastname: Schenkel
mesh_terms: D000818:Animals; D002458:Cell Fractionation; D002499:Centrifugation, Density Gradient; D002500:Centrifugation, Isopycnic; D004331:Drosophila melanogaster / Q000737:chemistry* / Q000196:embryology; D004492:Edetic Acid / Q000378:metabolism; D004533:Egtazic Acid / Q000378:metabolism; D004625:Embryo, Nonmammalian / Q000737:chemistry; D005615:Freezing; D034441:Heterogeneous-Nuclear Ribonucleoproteins; D012260:Ribonucleases / Q000037:antagonists & inhibitors; D012261:Ribonucleoproteins / Q000302:isolation & purification*
chemical_list: D034441:Heterogeneous-Nuclear Ribonucleoproteins; D012261:Ribonucleoproteins; D004533:Egtazic Acid; D004492:Edetic Acid; D012260:Ribonucleases