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Biomedical subjects

B Baranowska

Publications and source records attributed to B Baranowska.

At least 19 recordsLinked to original sources

Enhanced testosterone in female patients with anorexia nervosa: its normalization after weight gain.

In order to elucidate the mechanism of disturbances of gonadal hormones secretion in anorexia nervosa 14 female patients were investigated. A control group also consisted of 14 women of the same age. The serum LH, progesterone, oestrogens: oestrone + oestradiol (Oe1 + Oe2), oestriol (Oe3) and testosterone were determined by radioimmunological methods. In patients with anorexia nervosa the serum testosterone and Oe3 concentrations were dramatically elevated, whereas LH, progesterone and Oe1 + Oe2 were decreased as compared with the control group. Considerable weight gain induced by cyproheptadine treatment caused a normalization of the serum testosterone and Oe3 concentrations in all the patients. A negative correlation between the testosterone level and the deficit in body weight was observed. The mechanism causing the dramatically high serum testosterone concentration in the female patients with anorexia nervosa is discussed.

Adolescent

Conversion of 3H-testosterone to dihydrotestosterone in human hypertrophic prostatic tissue.

The aim of the study was to develop a simple method for the determination of the conversion of testosterone to 5 alpha-dihydrotestosterone (5 alpha-DHT) after incubation of human hypertrophic prostatic tissue with 3H-testosterone. The mean conversion rate of 3H-testosterone to 5 alpha-DHT in hypertrophic prostatic tissue was found to be higher than in normal and carcinomatous tissue. The results indicate that androgen metabolism in the hypertrophic prostatic gland is enhanced.

Aged

Pyruvate kinase from human skeletal muscle.

A simple method is described for the isolation of crystalline pyruvate kinase from human skeletal muscle. The enzyme was purified by ammonium sulfate fractionation, heat treatment and crystallization. Two crystal forms of pyruvate kinase differing in solubility but not in specific activity were found. The homogenous enzyme preparations in triethanolamine buffer, pH 7.6 reveal at 25 degrees a specific activity of 245 U per mg protein, and of 340 U/mg in potassium phosphate buffer (50 mM). The enzyme is activated by inorganic phosphate and fructosediphosphate to the same extent, and inhibited non competetively by ammonium ion. The molecular weight as measured by gel filtration is 220,000 daltons and the enzyme molecule is composed of 4 subunits.

Chromatography, Gel