Optimal conditions and specificity of interaction of a distinct class of nonhistone chromosomal proteins with DNA. Academic Article

abstract

• A subclass of nonhistone chromatin proteins with high DNA affinity has been isolated from rat liver. The interaction of the isolated proteins with DNA in vitro was characterized utilizing a nitrocellulose filter binding technique. The temperature, time, concentration, ionic strength, and pH dependence were characterized. Optimal interaction was observed at 0.19 M naCl, pH 7.5 with a protein to DNA ratio of 13 (w/w). Equilibrium and kinetic competition experiments indicated that these proteins interact optimally with A-T rich and single-stranded DNA. The data also suggest that these proteins might affect the helixcoil transiton of DNA.

authors

• Thomas, Terry

published proceedings

• Biochemistry

altmetric score

• 3

author list (cited authors)

• Thomas, T. L., & Patel, G. L.

citation count

• 39

complete list of authors

• Thomas, TL||Patel, GL

publication date

• April 1976

publisher

• American Chemical Society (ACS)  Publisher

published in

• Biochemistry  Journal

keywords

• Animals
• Binding Sites
• Binding, Competitive
• Cations, Monovalent
• Chromosomes
• DNA
• Deoxyribonucleoproteins
• Hydrogen-Ion Concentration
• Kinetics
• Liver
• Macromolecular Substances
• Nucleoproteins
• Osmolar Concentration
• Protein Binding
• Rats
• Temperature

PubMed Central ID

• 4089

Digital Object Identifier (DOI)

• 10.1021/bi00652a019

start page

• 1481

end page

• 1489

volume

• 15

issue

• 7

URL

• http%3A%2F%2Fdx.doi.org%2F10.1021%2Fbi00652a019