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Flow birefringence and intrinsic viscosity of a T2 bacteriophage DNA–methylated bovine serum albumin complex
Author(s) -
Harrington Rodney E.,
Martin Kathleen V.
Publication year - 1969
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1969.360070502
Subject(s) - chemistry , flow birefringence , dna , bovine serum albumin , molecule , chemical physics , bacteriophage , intramolecular force , intrinsic viscosity , dispersity , thermodynamics , birefringence , viscosity , crystallography , biophysics , chromatography , polymer chemistry , stereochemistry , biochemistry , organic chemistry , optics , physics , escherichia coli , biology , gene , polymer
The flow birefringence, extinction angles, and intrinsic viscosity have been determined at low velocity gradients for a complex of T2 bacteriophage DNA and methylated serum albumin prepared in dilute solution to a stoichiometry of approximately 90 proteins per DNA molecule. Comparative data upon equivalent solutions of pure uncomplexed T2 DNA are also presented, and these data are completely in accord with the results of previous study. The experimental data are interpreted in terms of current dynamical theory and indicate that the complex has an essentially linear chain structure, consisting of approximately two DNA molecules, which is hydrodynamically indistinguishable from the pure DNA and that extensive internal or intramolecular binding in the complex does not occur. Although interpretation of the results is hampered by an apparent moderate degree of polydispersity in the complex preparations and by relatively large shear extrapolations, the data for both DNA and the complex are substantially in accord with dynamical theory for a nondraining bead subchain model having high kinetic segmental rigidity.