Abstract：
:Heterogeneous nuclear ribonucleoprotein particles (HnRNP) were separated in metrizamide density gradients, into two fractions migrating to 1.31 g ml-1 and 1.18 g ml-1, respectively. Proteins associated with each of these fractions were analysed by SDS-acrylamide gel electrophoresis. It is shown that the whole proteins extracted from these two metrizamide fractions exhibit clearly different electrophoretic patterns: 1.31 HnRNP particles contain as major polypeptide chains molecules with molecular weights ranging from 40,000 to 65,000, while major polypeptides of 1.18 HnRNP are banding in the 30,000-40,000 molecular weight region of the gels. Both fractions contain numerous other associated polypeptide chains whose molecular weights are above 65,000. A possible kinetic relationship between these two HnRNP classes was investigated in vivo by performing chase experiments. No clear evidence for a precursor-product relationship was found. Implications arising from these structural and kinetic observations, and problems relating to nuclear maturation of pre-messenger RNA, are discussed.
journal_name
Mol Biol Repjournal_title
Molecular biology reportsauthors
Houssais JFdoi
10.1007/BF00643481subject
Has Abstractpub_date
1977-03-01 00:00:00pages
251-61issue
3eissn
0301-4851issn
1573-4978journal_volume
3pub_type
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