OBSERVATIONS CONCERNING THE BINDING OF THYROID HORMONES BY HUMAN SERUM PREALBUMIN*
Journal of Clinical InvestigationPublished 1 February 1963Open access
Sidney H. Ingbar
Citations126
SJR quartileQ1
SJR score4.72
SNIP2.17
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Keywords
Biochemistry, Genetics and Molecular Biology
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The thyroxine-serum protein complexes have been studied by means of electrophoresis at pH 8.6 using starch gel and paper as a supporting medium and there is a variation in the position of Band 1 and in the fastest moving prealbumin protein which may constitute a polymorphic system.
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In vitro experiments, performed at pH 7.4 and with a physiologic concentration of hormone, favor a role for prealbumin in the binding of thyroxine, suggesting that pre albumin is a specific fraction of the serum proteins and is not an artifact produced by certain buffer systems.
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From chemical and immunological observations, it was concluded that the tryptophanrich prealbumin, present as a complex in the α-globulin fraction, might be responsible for much of thyroxine-binding in human serum and the experiments to be described support this conclusion and throw further light on the nature of the thyroxin-binding globulin in human Serum.
