Reproductive outcome after cesarean scar pregnancy: A systematic review and meta-analysis.

Introduction: To evaluate subsequent reproductive among women with a prior cesarean scar pregnancy (CSP).

Material And Methods: MEDLINE, Embase and ClinicalTrials.gov databases were searched.

Quantitative structure-activity relationships in dihydropteroate synthase inhibition by multisubstituted sulfones. Design and synthesis of some new derivatives with improved potency.

On the bases of the linear correlation existing for a training set of homomultisubstituted 4-aminodiphenyl sulfones between the computed (INDO) electronic net charges of the SO2 group and the enzymic inhibition data on dihydropteroate synthase from Escherichia coli, seven new heteromultisubstituted derivatives were designed, synthesized, and tested for their inhibition potencies. These compounds were found to be from 5-11 times more effective than 4,4'-diaminodiphenyl sulfone. The implications of the results in the drug design and in the model for the enzyme-inhibitors interaction are discussed.

Quantitative structure-activity analysis in dihydropteroate synthase inhibition by sulfones. Comparison with sulfanilamides.

A set of 25 4'-, eight 2',4'-, and five 2',4',6'-substituted 4-aminodiphenyl sulfones were tested for their inhibitory activity on dihydropteroate synthase of Escherichia coli. Linear regression analysis shows that enzymic inhibition indices correlate well with both quantum chemical and spectroscopic descriptors of the electronic structure of the common moiety 4-NH2-C6H4-SO2 of the sulfones (the above descriptors being expressed in relation to the electronic structure of the enzyme substrate, p-aminobenzoate). Therefore, the biological activity of the sulfones can be related to the electronic structural resemblance between these inhibitors and the substrate of the target enzyme.

Structure-activity relationships in dihydropteroate synthase inhibition by sulfanilamides. Comparison with the antibacterial activity.

A set of 12 acidic, 5 imidic, and 5 amidic sulfanilamides (SA) were tested for their inhibitory activity on dihydropteroate synthase of Escherichia coli. The enzyme inhibition indexes (EII50) were compared with the growth inhibition indexes (GII50), and electronic structures of SA and cell permeability effects were discussed as possible determinant factors of the observed variation of the activity in the SA set. The results strongly support the following conclusion: (a) permeability factors are highly effective in depressing the activity of SA in growth inhibition with respect to enzyme inhibition, but they do not appear to contribute significantly to the activity variation; (b) the activities of the different SA, both in growth and enzyme inhibition experiments, are well accounted for by the electronic features of these compounds.

[Effect of surgical stress on TSH and on the extra-thyroid metabolism of T4 (preliminary experiment)].

The effect of the surgery on the TSH and on the extra thyroid T4 metabolism was studied in thirty euthyroid patients. The TSH showed a light increase thirty minutes after the skin cut. There were no remarkable changes of T4 serum levels, while the serum triiodothyronine concentration fell during and after the operation, with a concomitant rise in reverse triiodothyronine.

Developmental changes of rat liver cytoplasmic and mitochondrial aconitate hydratases.

The developmental patterns of the activity of cytoplasmic and mitochondrial aconitate hydratses of rat liver have been studied. Both activities are low in foetal liver, with respect to adult levels, and begin to increase after birth. The activity of the mitochondrial enzyme reaches a maximum about two days after birth, then decreasing gradually to adult level.

Kinetic studies of cytoplasmic and mitochondrial aconitate hydratases from rat liver.

The kinetic properties of the cytoplasmic and mitochondrial aconitate hydratases of rat liver have been studied by measuring the formation of the two products from each of the three tricarboxylic acids used as substrate. The kinetic properties of the two enzymes are very similar; the similarity of the Km values for each of the three substrates is particularly remarkable. The results are discussed with particular reference to a possible role of the cytoplasmic aconitate hydratase in the process of gluconeogenesis.

Affinity chromatography of yeast nicotinamide-adenine dinucleotide-specific isocitrate dehydrogenase on immobilized nicotinamide-adenine dinucleotide. Effects of ligands.

The method of affinity chromatography has been used for studying the effects of some ligands of yeast NAD-specific isocitrate dehydrogenase on the affinity of the enzyme for NAD+ immobilized on Sepharose 4B. In absence of ligands, the enzyme is eluted from NAD+-Sepharose columns by 0.1 M phosphate buffer, pH 7.

Polymeric forms of yeast nicotinamide-adenine dinucleotide-specific isocitrate dehydrogenase in the presence of various ligands.

The molecular weight of NAD-specific isocitrate dehydrogenase, purified from baker's yeast, has been studied by molecular sieve chromatography. By elution of the enzyme from columns of Sepharose 6B with 0.05 M phosphate buffer, pH 7.

Effect of pH on the inhibition of the nicotinamide-adenine dinucleotide-specific isocitrate dehydrogenase from baker's yeast by anions.

1. The sensitivity of the NAD(+)-specific isocitrate dehydrogenase from baker's yeast towards inhibition by anions decreases with decrease in pH. The patterns of the pH-dependence of the enzymic activity can be explained by this effect.