Classification and purification of proteins of heterogeneous nuclear ribonucleoprotein particles by RNA-binding specificities
Several proteins of heterogeneous nuclear ribonucleoprotein (hnRNP) particles display very high binding affinities for different ribonucleotide homopolymers. The specificity of some of these proteins at high salt concentrations and in the presence of heparin allows for their rapid one-step purification from HeLa nucleoplasm. The authors show that the hnRNP proteins are poly(U)-binding proteins and compare their specificity to that of the previously described cytoplasmic poly(A)-binding protein. These findings provide a useful tool for the classification and purification of hnRNP proteins from various tissues and organisms and indicate that different hnRNP proteins have different RNA-binding specificities.
- Research Organization:
- Dept. of Biochemistry, Molecular Biology, and Cell Biology, Northwestern Univ., Evanston, IL (US)
- OSTI ID:
- 7192106
- Journal Information:
- Mol. Cell. Biol.; (United States), Vol. 8:5
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
37 INORGANIC
ORGANIC
PHYSICAL AND ANALYTICAL CHEMISTRY
NUCLEOPROTEINS
CLASSIFICATION
BIOCHEMICAL REACTION KINETICS
CHEMICAL BONDS
HELA CELLS
HEPARIN
PURIFICATION
RNA
SEPARATION PROCESSES
SPECIFICITY
AMINES
ANTICOAGULANTS
CARBOHYDRATES
DRUGS
HEMATOLOGIC AGENTS
KINETICS
MUCOPOLYSACCHARIDES
NUCLEIC ACIDS
ORGANIC COMPOUNDS
ORGANIC SULFUR COMPOUNDS
POLYSACCHARIDES
PROTEINS
REACTION KINETICS
SACCHARIDES
550200* - Biochemistry
400201 - Chemical & Physicochemical Properties