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Binding of globular proteins to DNA from surface tension measurement

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Title Binding of globular proteins to DNA from surface tension measurement
 
Creator Mitra, A
Chattoraj, D K
Chakraborty, P
 
Description 313-320
Extent of binding (Гp)
of globular proteins to calf-thymus DNA have been measured in mole per mole of
nucleotide as function of equilibrium protein concentration. We have exploited
measurement of the surface tension of the protein solution in the presence and
absence of DNA to calculate the binding ration (Гp). Interaction of bovine
serum albumin with DNA has been studied at different pH. Interaction of bovine serum albumin with DNA has been studied
at different pH, ionic strength and
in presence of Ca2+. Interaction of GSA with denatured DNA has also
been in vestigated. Binding isotherms for other globular proteins like b-lactoglobulin, α-lactalbumin and lysozyme have been compared
under identical physicochemical condition. It has been noted with considerable
interest that globular form of protein is important to some extent in protein-DNA
interaction. An attempt has been made to explain the significance of difference
in binding ratios of these two biopolymers in aqueous medium for different
systems in the light of electrostatic and hydrophobic effects. Values of maximum
binding ration (Гpm) at saturated level for different systems have
been also presented. The Gibb's free energy decrease (-∆G0) of the
binding of proteins to DNA has been compared more precisely for the saturation of
binding sites in the DNA with the change of activity of protein in solution
from zero to unity in the rational mole fraction scale.
 
Date 2012-12-25T18:32:46Z
2012-12-25T18:32:46Z
2001-10
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/15309
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.38(5) [October 2001]