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Growth hormone (GH) and prolactin (PRL) responses after TRH administration were studied in 31 women presenting with the clinical, biochemical and ultrasonographic characteristics of the polycystic ovarian (PCO) syndrome; their results were compared with those of 20 normally menstruating women investigated during the early follicular phase of the cycle. Based on the GH responses two PCO subgroups were observed: (a) nonresponders (n = 16) who showed △max GH responses (0.7 ± 0.27 ng/ml, x ± SE) similar to those of the normals (0.97 ± 0.20 ng/ml), and (b) responders (n = 15), 48.4% of the PCO patients who showed a paradoxical increase in GH levels (△max GH, 18.0 ± 1.96 ng/ml) following thyrotropin-releasing hormone (TRH) administration significantly higher than those observed either in nonresponder PCO patients or in normals. Furthermore, basal GH levels were found to be significantly higher in the responder PCO subgroup (5.65 ± 0.75 ng/ml) compared to either nonresponders (1.58 ± 0.21 ng/ml) or normals (1.8 ± 0.18 ng/ml). However, no correlation was found between basal GH levels and △max GH responses observed. Additionally, basal PRL and △max PRL levels following TRH administration did not differ either between the two PCO subgroups or those observed in normal controls. Δ₄A, T and E₂ levels were similar between the two PCO subgroups. No correlation was found between the △max GH responses to △max PRL or the post-luteinizing hormone-releasing hormone stimulation test △max luteinizing hormone:follicle-stimulating hormone ratio observed or to steroid levels. These data are suggestive of an abnormal responsiveness of somatotrophs to TRH stimulation in 48.4% of PCO patients which could not be correlated either with an abnormality of lactotrophs or with a difference of the androgen and E₂ levels.

The transferrins are a group of iron-binding glucoproteins migrating in the 3-globulin region on starch gel electrophoresis (Smithies and Hiller, i959 sliced into three layers; the upper layer was not used, the middle layer was stained with amido-black io-B to reveal proteins, and the lower one was used for the detection of transferrins by autoradiography. The Nitroso-R reagent of Smithies (1959) was also used to check the identity of the variants as iron-binding proteins. Results and DiscussionIn 204I out of the 2050 people examined only transferrin C was found. In 6 Greeks a slow transferrin band was found in addition to transferrin C, while in 3 persons a faster-migrating band besides transferrin C was noticed. Therefore, 204I (99-56%) people were of phenotype CC, 6 (0o29%) of phenotype CD1, and 3 (o0I5%) subjects were of phenotype CB2.On our findings the frequency of gene TfC is 0o9978 in the Greek population, of gene TfD1 it is -000I5, and of gene TfB2 it is o0007.No case of atransferrinaemia among the 2050 tested specimens was noticed. In IO sera specimens no migration of radioactive iron to the anode during electrophoresis was observed. These sera have been preserved in deep freeze for more than six months. When fresh collected blood specimens from the same subjects were tested again, the migration of the radioactive iron was perfect and the IO sera were found to be homozygous for transferrin C. We believe that denaturation of the iron-binding globulin during long preservation in low temperature is responsible for this phenomenon.

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