Proceedings of the National Academy of Sciences · 1973 · 31 citations · 24 references
Life SciencesBiochemistryMolecular BiologyChromatin BiologyChromatin StructureNucleic Acid BiochemistryChromatinChromatin InteractionsNucleic Acid RecognitionNucleic Acid-protein InteractionsProtein-nucleic Acid InteractionsChromatin-associated Protein InteractionsIonic StrengthIonic Strength DependenceIonic Strength EffectsNucleic Acid Binding AffinityNucleic Acid Binding SpecificityNucleic Acid Interactions With Proteins
A fraction of chromatin acidic protein from rat liver, predominantly comprised of low-molecular-weight species, showed highest in vitro affinity for DNA when compared with other fractions of nuclear acidic protein. Maximum binding of this protein fraction was observed at physiological ionic strength of 0.14 M NaCl and DNA/protein ratio > 1. Comparison of their binding to homologous and heterologous DNAs showed partial species specificity. All molecular species of this protein fraction appear to bind to DNA.
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Current topics in developmental biology
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Studies of Nuclear Acidic Proteins
C S Teng, Ching-Sung Teng, V. G. Allfrey · Journal of Biological Chemistry · 1971 · 495 citations · Full text
W Gilbert, Benno Müller‐Hill · Proceedings of the National Academy of Sciences · 1967 · 305 citations · Full text
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Specific Binding of the λ Phage Repressor to λ DNA
Mark Ptashne · Nature · 1967 · 261 citations