ISSN:
0022-3832
Keywords:
Chemistry
;
Polymer and Materials Science
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Chemistry and Pharmacology
,
Physics
Notes:
The hydrodynamic properties of native and urea-denatured fibrinogen have been investigated, primarily to examine further the suggestion, based on a consideration of data for horse serum albumin, that urea denaturation may involve swelling instead of increased asymmetry. A sedimentation-diffusion and also a light scattering molecular weight determination at the isoelectric point indicate that 6 M urea causes neither splitting nor aggregation of the native protein in the denaturation process. The observed increase in the intrinsic viscosity and frictional coefficient upon denaturation can be interpreted in terms of an equivalent hydrodynamic ellipsoid of approximately the same shape but of a volume which is approximately 1.7 times that for the native protein. The effective volume appears to be slightly dependent on pH with a minimum at the isoelectric point. It thus appears that the urea denaturation of bovine fibrinogen, like that of horse serum albumin, may involve swelling. There is no indication in the case of either protein that increased asymmetry is involved in accounting for the frictional behavior of the denatured substances.
Additional Material:
7 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/pol.1954.120147702
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