Improvement in botanical standardization of commercial freeze-dried herbal extracts by using the combination of antioxidant capacity and constituent marker concentrations.

Botanical extracts are standardized to > or = 1 marker compounds (MCs). This standardization provides a certain level of quality control, but not complete quality assurance. Thus, industries are looking for other satisfactory systems to improve standardization.

Characterization and biological activity of the main flavonoids from Swiss Chard (Beta vulgaris subspecies cycla).

The molecular components of a phenolic fraction (P2), obtained from liquid chromatography of a Swiss Chard (Beta vulgaris subsp. cycla) extract, were identified using HPLC-ESI-MS/MS. The primary P2 components were: vitexin-2''O-rhamnoside, its demethylated form 2''-xylosylvitexin, isorhamnetin 3-gentiobioside, and rutin.

Glucose-6-phosphate dehydrogenase and NADPH-consuming enzymes in the rat olfactory bulb.

The resistance to oxidative stress is a multifactorial reaction involving the clustering of transcriptionally regulated genes. Because glucose-6-phosphate dehydrogenase (G6PD), the principal enzyme responsible for reducing power, is highly expressed in the olfactory bulb (OB), it is of interest to verify whether other enzymes utilizing NADPH are also highly expressed. The level and localization of G6PD- and NADPH-consuming enzymes, such as NADPH-cytochrome P450 oxidoreductase (P450R), glutathione reductase (GR), and NADPH-diaphorase (NADPH-d), were analyzed in the rat olfactory bulb (OB) by quantitative histochemistry and immunohistochemistry.

NADPH-consuming enzymes correlate with glucose-6-phosphate dehydrogenase in Purkinje cells: an immunohistochemical and enzyme histochemical study of the rat cerebellar cortex.

In cerebellum of the adult rat, glucose-6-phosphate dehydrogenase (G6PD) activity is particularly localized in Purkinje cells, showing lower activity in the molecular and granule cell layers. G6PD is the first and rate-limiting step of the hexose monophosphate shunt (HMS), which has the physiological role of providing NADPH for reductive biosynthesis and detoxifying reactions. In this study, we searched for a possible correlation between G6PD and other NADPH-consuming enzymes, such as NADPH-cytochrome P450 reductase (P450R), glutathione reductase (GR) and NADPH-diaphorase (NADPH-d).

Glucose-6-phosphate dehydrogenase expression associated with NADPH-dependent reactions in cerebellar neurons.

This review describes the variation of glucose-6-phosphate dehydrogenase (G6PD) activity in the main neurons of the molecular and granular layers as well as in the deep nuclei of the cerebellum as observed so far by optical and electron microscopy studies. Light microscopy and semiquantitative microphotometry of histochemical staining showed that the highest G6PD activity was expressed by Purkinje cells and neurons of the deep cerebellar nuclei; the elements of the molecular layer showed a diffuse G6PD staining, while the granular layer displayed only scattered G6PD activity. Electron microscopy analysis showed that the basket and stellate cells, as well as the Golgi cells, have a remarkable G6PD activity, while in the granule cells the enzyme was barely detectable.