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Ribonucleoprotein particles have been isolated from duck erythroblast nuclei using a procedure designed to produce maximal cytoplasmic dispersion with minimal release of endogenous hydrolytic enzymes. The RNA extracted from the purified nuclear ribonucleoprotein fraction is shown to contain globin messenger RNA sequences at a concentration comparable to that present in total nuclear RNA. The polypeptide composition of this fraction revealed by electrophoresis in two dimensions is complex, consisting of at least 65 acidic species and 21 basic species. Several lines of evidence suggest that these are authentic components of nuclear ribonucleoprotein. The so-called 'core' proteins of nuclear ribonucleoprotein which were previously shown to migrate as a single band on low-pH urea gels, and as six bands on sodium dodecyl sulphate gels are here shown to be considerably more complex being resolved by two-dimensional electrophoresis into a group of 15 basic and 6 more and less neutral polypeptides. Isoelectric focusing of nuclear ribonucleoprotein under non-denaturing conditions suggests that these latter species are not uniformly distributed along the pre-messenger RNA molecule.
K Maundrell, and
K Scherrer
October 1975,
Molecular biology reports,
K Maundrell, and
K Scherrer
October 1980,
The Journal of cell biology,
K Maundrell, and
K Scherrer
June 1966,
Nature,
K Maundrell, and
K Scherrer
October 1973,
European journal of biochemistry,
K Maundrell, and
K Scherrer
January 1978,
Methods in cell biology,
K Maundrell, and
K Scherrer
January 1977,
Molekuliarnaia biologiia,
K Maundrell, and
K Scherrer
January 1990,
Molecular biology reports,
K Maundrell, and
K Scherrer
August 1976,
Cell,
K Maundrell, and
K Scherrer
April 1973,
Proceedings of the National Academy of Sciences of the United States of America,
K Maundrell, and
K Scherrer
June 1985,
The EMBO journal,
