Effects of freezing on the estimated amounts of Tamm–Horsfall glycoprotein in urine, as determined by radioimmunoassay

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Abstract
Freeze-drying or freezing of salt-free solutions of human Tamm-Horsfall glycoprotein apparently lead to changes in the structure of the latter, changes that increased its ability to bind with antibody raised, in rabbits, against it. This alteration in avidity of the glycoprotein was observed irrespective of whether antiserum was raised against freeze-dried or non-frozen antigen. The implications of this finding for the radioimmunoassay of the glycoprotein in urine samples were studied. Appropriate treatment for urine samples, before assay, was devised. The amount of Tamm-Horsfall glycoprotein excreted ranged from 30-138 mg in normal males and 43-126 mg in normal females/24 h.