Possible importance of thyroidal iodine compartments in the adaptation of thyroid hormone secretion to antithyroid drugs.
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Biomedical subjects
Publications and source records attributed to H Kohler.
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The variable regions of the light and heavy chains on the same macroglobulin (immunoglobulin M) molecule are no more related in amino acid sequence than are the variable regions of the light and heavy chains of different immunoglobulin molecules. Subgroups of micro chains are similar in their variable sequence to subgroups of gamma chains.
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Among new insights coming from the completion of sequencing of the human genome, reported in Nature and Science, are clues of how evolution has increased the complexity of species, and in particular how the genetic code has enabled this process. It is clear that life has not only evolved by increasing the number of genes, but also by ingeniously evolving an efficient code for expressing diversity in the building blocks (i.e. the amino acids). The rules of nucleic acid base pairing and the classification of amino acids according to hydrophobicity/hydrophilicity relationships define a binary DNA code, which determines the general biophysical characteristics of proteins. Sense and antisense strands can encode protein segments having inverted and complementary hydropathy. The underlying binary code controls association and dissociation of proteins and presumably represents a primordial code that might have emerged in the early stages of self-organizing biochemical cycles. It is the purpose of this communication to provide a perspective of the code in the context of a binary language from its primordial origin to its present day format and to propose to use this code as a genomic mining tool.
Eight patients with terminal renal failure (GFR less than 5 ml/min) received guanfacine intravenously or orally at the beginning of a haemodialysis session lasting 5 hours. After intravenous administration the elimination rate constant of the unchanged drug was calculated to be 0.59 h-1, corresponding to an elimination half-life of about 12 h, which is similar to the values of patients with normal renal function. Following oral ingestion, only 2.4% of the guanfacine dose administered were extracted unchanged in the dialysate during the haemodialysis period. The clearance by dialysis was 53 ml/min for guanfacine, which represents about 15% of the total clearance of guanfacine reported in the literature. The low dialysis clearance of guanfacine is consistent with the high rate of biotransformation of the drug and its binding to red blood cells and plasma proteins. Thus guanfacine may be dosed independently of haemodialysis treatment periods.