Accession Number:

AD0257793

Title:

THE PROPERTIES OF THYROGLOBULIN. VI. THE INTERNAL RIGIDITY OF NATIVE AND DENATURED THYROGLOBULIN

Descriptive Note:

Corporate Author:

NAVAL MEDICAL RESEARCH INST BETHESDA MD

Personal Author(s):

Report Date:

1960-11-04

Pagination or Media Count:

1.0

Abstract:

The rotational relaxation time of native thyroglobulin has been evaluated from polarization measurements of thyroglobulin coupled to a fluorescent dye. By treatment with detergent or urea the relaxation time of thyroglobulin was markedly reduced. The original polarization was recovered on dilution out of either reagent. The disruption of the internal structure produced by detergent was evident by the ability of sulfhydryl reagents to further decrease the relaxation time whereas they are without effect in the absence of detergent. Similarly a time-dependent decrease in polarization was evident in alkali when 8M urea or 5M guanidine was present. In the absence of the latter reagent only a relatively small change in relaxation time occurred in alkali. The changes in polarization have been compared with hydrodynamic methods acertaining configurational modifications. It is apparent that polarization measurements can provide additional insight into the degree of disorganization of the internal structure of a protein molecule. Author

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Distribution Statement:

APPROVED FOR PUBLIC RELEASE