Therapeutic activity of Physioquens in the treatment of certain gynecological conditions (author's transl)]

The new hormonal preparation Physioquens was administered during the study to 181 women during 1.634 cycles and has proved to be very effective in the treatment of various gynaecological disturbances. A definitive reduction has been observed in premenstrual and pre and postmenopausal complaints, dysmenorrhoea, amenorrhoea, intermenstrual pain and endometriosis. Physiquens is also a perfect regulatory device of the cycle in the case of menorrhagia, metrorrhagia and irregular menstrual cycles connected with a hormonal insufficiency. The normophasic treatment with Physioquens is made up of the cyclical administration of a tablet of 0.050 mg ethinyloestradiol for the first 7 days, followed by a tablet of 1 mg lynestrenol and 0.050 mg ethinyloestradiol for the next 15 days. Because of its effectiveness and good tolerance both clinically and biologically Physioquens can be considered an important new step in the treatment of gynaecological problems.     

Modification of the alkali light chains of skeletal myosin inhibits actin binding and adenosine triphosphate cleavage.

Heavy meromyosin treated with the ATP analog, 6,6'-dithiobis(inosinyl-5'-yl imidodiphosphate), (slppNHp)2, in the presence of adenyl-5'-yl imidodiphosphate at 0 degrees loses its EDTA-ATPase activity and actin binding ability in a parallel manner. Studies with myosin show that under the above conditions (slppNHp)2 reacts preferentially with the single cysteines of the alkali light chains (Mr = 20,700 and 16,500) suggesting a role for these subunits in regulating actin-myosin interaction and ATP cleavage.     

Leishmania tarentolae: proline anabolism in promastigotes.

Using ¹⁴C-labeled substrates in conjunction with thin-layer Chromatographic radioautography, studies were done to determine the precursors for proline synthesis utilized by promastigotes of Leishmania tarentolae. The only substances in Trager's Defined Medium capable of acting as proline precursors under the conditions studied were l-arginine and l-ornithine. None of the other substrates tested (16 amino acids, five purines and pyrimidines, and glucose) were converted to proline. l-glutamate, l-aspartate, and d-glucose did not act as precursors for the imino acid although they stimulated oxygen uptake better than did l-arginine and l-ornithine. Proline synthesis was unaffected by the presence of preformed proline indicating the absence of end product feedback inhibition.     

Purification and characterization of N-methylalanine dehydrogenase.

Cell free extracts of Pseudomonas MS previously have been shown to carry out the synthesis of a novel amino acid, N-methylalanine (Kung, H.F., and Wagner, C. (1970) Biochim. Biophys. Acta 201, 513-516). An enzyme has been isolated from this organism which is responsible for the synthesis of N-methylalanine. The stoichiometry of the reaction catalyzed by this enzyme leads to the following formulation: Methylamine + pyruvate + NADPH + H-+ yields N-methylalanine + NADP-+ + H2O. This enzyme has been physically separated from alanine dehydrogenase, which is also present in these extracts. This new enzyme has been named N-methylalanine dehydrogenase. It has been purified to near homogeneity as judged by disc gel electrophoresis. Gel filtration chromatography showed that N-methylalanine dehydrogenase has an apparent molecular weight of 77,000, while electrophoresis in sodium dodecyl sulfate gave rise to a single band with a molecular weight of approximately 36,500. The enzyme is optimally active in the pH range between 8.2 and 8.6. The apparent K-m values for pyruvate, NADPH, and methylamine, respectively, are 1-5 times 10 minus 2 M, 3-5 times 10 minus 5 M, and 7.5 times 10 minus 2 M.     

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