A histochemical study of δ5-3Β-hydroxysteroid dehydrogenase activity in the interstitial cells of the mammalian ovary

Riassunto Le cellule interstiziali dell'ovaio presentano spiccata attività enzimatica (3-OHD) ed organizzazione submicroscopica tipicamente stereidogenica nella donna nel periodo fetale e nel ciclo mestruale; nel ratto e nella cavia nel ciclo estrale e nella gravidanza. Negli stessi mammiferi tale attività è équivalente e coordinata a quella della teca interna e del corpo luteo.     

Histochemical localization of glutamic acid dehydrogenase activity in the cuneate nucleus of the cat1

Summary Glutamic acid dehydrogenase activity was observed both in the neuropil as well as in several classes of cuneate neurons in the cat.The excellent technical assistance of Mr. C. T. Lee of our Histology Laboratory, and the support and encouragement of Professor W. C. Wong, Anatomy Department, are gratefully acknowledged.     

Distribution of procoagulant activity in the subcellular fractions of human granulocytes

Résumé Les extraits granulocytaires racourcissent le temps de coagulation de plasmas déficients en facteurs VIII, IX et XII. Une activité paracoagulante particulièrement élevée se manifeste dans les subfractions de granulocytes contenant des lysosomes et d'autres structures cytoplasmatiques.     

A histochemical study of succinic dehydrogenase activity in rat liver cancerogenesis induced by 3-methyl-4-dimethylaminoazobenzene

Résumé L'auteur a étudié histochimiquement l'activité de la succine déhydrogénase lors de la cancérogénèse expérimentale du foie des rats induite par le 3'-méthyl-4-diméthylaminoazobenzène. On a observé une augmentation de l'activité enzymatique dans les stades précancéreux (cholangiofibrose et hypertrophie parenchymateuse) suivie d'une diminution et disparition de cette activité dans les tumeurs développés.     

S-nitrosoglutathione reductase activity of human and yeast glutathione-dependent formaldehyde dehydrogenase and its nuclear and cytoplasmic localisation

S-nitrosoglutathione (GSNO) formation represents a mechanism for storage and transport of nitric oxide. Analysis of human liver and Saccharomyces cerevisiae extracts has revealed the presence of only one enzyme able to significantly reduce GSNO, identified as glutathione-dependent formaldehyde dehydrogenase (FALDH). GSNO is the best substrate known for the human and yeast enzymes (kcat/Km = 444,400 and 350,000 mM(-1) min(-1), respectively). Although NADH is the preferred cofactor, some activity with NADPH (Km = 460 microM) can be predicted in vivo. The subcellular localization demonstrates a cytosolic and nuclear distribution of FALDH in living yeast cells. This agrees with previous results in rat, and suggests a role in the regulation of GSNO levels in the cytoplasmic and nuclear compartments of the eukaryotic cell.     

3'5'-Cyclic AMP phosphodiesterase activity in the internal and external layers of human myometrium at the end of pregnancy]

The hydrolysis of cAMP by phosphodiesterase was studied in whole homogenate from human myometrium at the end of the pregnancy before onset of labour. Tissue samples were taken from outer and inner layers of placental and anti-placental sites. Kinetic analysis shows in every case two apparent Km values for low and high cAMP concentrations in the order of 1 x 10(-5) M and 1 x 10(-4) M. On the other hand Vmax values are lower for the enzyme isolated from the placental site than for the one isolated from the anti-placental area. In the 4 zones studied, an appreciable proportion of the low Km enzyme is present.     

Quantitative distribution of glucose-6-phosphate dehydrogenase and isocitric dehydrogenase in the human nephron

Zusammenfassung In den einzelnen Abschnitten des menschlichen Nephrons und in Nierenhomogenaten wurden quantitativ die Glucose-6-phosphat-dehydrogenase-und die Isozitronens?uredehydrogenase-Aktivit?t gemessen.

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This investigation was made possible by a grant from the Swiss National Foundation for the Development of Scientific Research. The technical assistance of MissD. Keller is gratefully acknowledged.     

Enrichment of ligands with molecular dockings and subsequent characterization for human alcohol dehydrogenase 3

Alcohol dehydrogenase 3 (ADH3) has been assigned a role in nitric oxide homeostasis due to its function as an S-nitrosoglutathione reductase. As altered S-nitrosoglutathione levels are often associated with disease, compounds that modulate ADH3 activity might be of therapeutic interest. We performed a virtual screening with molecular dockings of more than 40,000 compounds into the active site of human ADH3. A novel knowledge-based scoring method was used to rank compounds, and several compounds that were not known to interact with ADH3 were tested in vitro. Two of these showed substrate activity (9-decen-1-ol and dodecyltetraglycol), where calculated binding scoring energies correlated well with the logarithm of the k _cat/K _m values for the substrates. Two compounds showed inhibition capacity (deoxycholic acid and doxorubicin), and with these data three different lines for specific inhibitors for ADH3 are suggested: fatty acids, glutathione analogs, and cholic acids.