Open AccessGENETIC POLYMORPHISM OF RHESUS THYROXINE-BINDING PREALBUMIN: EVIDENCE FOR TETRAMERIC STRUCTURE IN PRIMATES
Author(s) -
Chester A. Alper,
Noel I. Robin,
Samuel Refetoff
Publication year - 1969
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.63.3.775
Subject(s) - transthyretin , tetramer , biology , allele , agarose , agarose gel electrophoresis , polymorphism (computer science) , microbiology and biotechnology , bovine serum albumin , genetics , biochemistry , endocrinology , dna , gene , enzyme
Polymorphism in primate thyroxine-binding prealbumin was investigated with agarose gel electrophoresis at pH 8.6. In the rhesus monkey (Macaca mulatta ), three forms of this protein were found in random sera: a single rapidly migrating band similar to that in human and other primate sera, a single slowly migrating band cathodal to rhesus albumin, and a five-banded form, the most rapid and slowest bands of which corresponded to the other two forms. The frequencies of occurrence of these three forms were consistent with the hypotheses that rhesus prealbumin is under the control of two codominant autosomal alleles,PAF andPAS , and that the protein occurs naturally in serum as a tetramer composed of similar subunits.It was possible, by simple mixingin vitro , to produce five-banded prealbumin patterns from rhesus PA SS serum and rhesus PA FF serum,M. arctoides serum,P. hamadryas serum, and human serum. Thyroxine was bound by all the hybrid molecules produced in this fashion.