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Biomedical subjects

E Kallee

Publications and source records attributed to E Kallee.

At least 37 records · Page 2Linked to original sources
PubMed1978

[Familial coincidence of hypertrophic cardiomyopathies and thyroxine-binding globulin deficiency (athyropexinemia) (author's transl)].

A twenty-five year old man was found to have simultaneous total deficiency of thyroxine-binding globulin ("thyropexin") and hereditary hypertrophic obstructive cardiomyopathy (HOCM). The thyroxine-binding capacity (RT3U), thyroid hormone levels, PB127I, PB131I and TBG (RIA) in serum were very low and TBG cap was zero. Trapping of radioiodine in the thyroid was enhanced. Clinically, the patient appeared euthyroid. The case seems to be similar to another one described earlier by Ingbar. An investigation of the family showed that in one uncle and two nephews of the patient thyropexin was absent whilst the mother, one sister and one female cousin had partial thyropexin deficiencies. One of these nephews also suffers from asymmetric septal hypertrophy (ASH), the mother of the propositus has a non-obstructive hypertrophic cardiomyopathy (HCM).

Adult↗
PubMed1978

[Thromboplastin activity of extracts of human thyroid glands (author's transl)].

Aqueous extracts of thyroid glands were prepared from 25 surgical specimens of 19 patients. The average prothrombin time of sixteen 3:4 diluted extracts of thyroids from 13 euthyroid patients was 16.8 +/- 2.3 sec as measured with 100% human plasma. Under similar conditions the average prothrombin time of extracts obtained from the grey matter of three human brains was 18.4 +/- 0.3 sec. The thyroid may thus be considered as an organ containing one of the highest concentrations of tissue thromboplastin.

Humans↗
PubMed1977

Adsorption equilibria of thyroid hormones in the liver cell.

The adsorptive distribution of L-thyroxine and L-triiodothyronine at 0.04--25nM concentrations was determined in suspensions of mitochondria in soluble cytoplasmic proteins from rat livers, at protein concentrations of 0.5--4.7 mg total protein/ml suspension. In the concentration ranges measured no saturation of both mitochondria and soluble proteins with thyroid hormones could be observed. The distribution of the hormones between the liquid phase of cytoplasmic proteins and the solid phase of the mitochondria depended mainly on the ratio of the amounts of proteins in both phases. Certain drugs such as chlorpromazine and phenobarbital in concentrations used therapeutically can interfere with the processes of adsorptive transport in vitro. Chlorpromazine, in the presence of desorptively functioning cytoplasmic proteins or serum proteins, promotes the adsorption of thyroxine and triiodothyronine onto the mitochondria. In contrast, phenobarbital weakens the binding of the hormones to the mitochondria. The processes of adsorptive binding of thyroid hormones to cell proteins in vitro are suggested as possible links in a transport chain between different compartments in vivo. The new model may also explain the effect of drugs on the distribution of thyroid hormones within the cell.

Adsorption↗