Differences in the binding of thyroid hormones and indoles by rat alpha 1-fetoprotein and serum albumin.
The transport of small molecules in the blood, normally assured by serum albumin in the adult, is not well known in the fetus since the albumin concentration is low in fetal serum and inversely related to the alpha 1-fetoprotein concentration. In order to investigate whether rat alpha 1-fetoprotein might be a fetal counterpart to albumin, the binding properties of these two proteins have been compared with respect to a series of molecules of biological importance, especially during fetal development: thyroid hormones and indole analogues. Though high-affinity binding of thyroxine was found with both rat alpha 1-fetoprotein and albumin, a significant difference in the number of binding sites for this hormone was found with the two proteins. Further, while rat serum albumin strongly bound L-tryptophan and indolyl-3-acetic acid (Ka approximately equal to 10(5) M-1), rat alpha 1-fetoprotein did not bind any of the indoles tested. These results are discussed with respect to the physiological and pharmacological significance of the transport role of these proteins.
D000818:Animals; D001692:Biological Transport; D007211:Indoles / Q000097:blood*; D011485:Protein Binding; D051381:Rats; D012709:Serum Albumin / Q000378:metabolism*; D013963:Thyroid Hormones / Q000097:blood*; D000509:alpha-Fetoproteins / Q000378:metabolism*
D007211:Indoles; D012709:Serum Albumin; D013963:Thyroid Hormones; D000509:alpha-Fetoproteins