Photoinhibition of Photosystem I in field-grown barley (Hordeum vulgare L.): Induction, recovery and acclimation.

The effects of exposure of a field-grown winter cultivar of barley (Hordeum vulgare L.) to Photosystem I (PS I) photoinhibitory conditions in the form of bright day-light combined with chilling conditions were investigated. PS I photoinhibition was manifested by damage to the Fe-S centers of PS I and to the PS I-A/B polypeptides. Up to 20% of the PS I complexes were photoinactivated. Upon transfer to room temperature, the plants partially recovered from PS I photoinhibition, although damage was still detectable after one week. These results demonstrate that PS I photoinhibition is a physiologically relevant phenomenon in chilling-tolerant plants grown under field conditions. In order to study the induction of cyclic electron transport around PS I by PS I photoinhibitory conditions, antibodies raised against the NDH-I subunit of the NDH complex (a component of cyclic electron transport) were used to measure NDH levels in the exposed plants. A marked increase in the amount of NDH complex and a corresponding increase in NADPH dehydrogenase activity in the thylakoids were observed. The data indicate that the response to PS I-photoinhibitory conditions may involve regulated changes in cyclic electron transport around PS I.

The NAD(P)H dehydrogenase in barley thylakoids is photoactivatable and uses NADPH as well as NADH

An improved light-dependent assay was used to characterize the NAD(P)H dehydrogenase (NDH) in thylakoids of barley (Hordeum vulgare L.). The enzyme was sensitive to rotenone, confirming the involvement of a complex I-type enzyme. NADPH and NADH were equally good substrates for the dehydrogenase. Maximum rates of activity were 10 to 19 &mgr;mol electrons mg-1 chlorophyll h-1, corresponding to about 3% of linear electron-transport rates, or to about 40% of ferredoxin-dependent cyclic electron-transport rates. The NDH was activated by light treatment. After photoactivation, a subsequent light-independent period of about 1 h was required for maximum activation. The NDH could also be activated by incubation of the thylakoids in low-ionic-strength buffer. The kinetics, substrate specificity, and inhibitor profiles were essentially the same for both induction strategies. The possible involvement of ferredoxin:NADP+ oxidoreductase (FNR) in the NDH activity could be excluded based on the lack of preference for NADPH over NADH. Furthermore, thenoyltrifluoroacetone inhibited the diaphorase activity of FNR but not the NDH activity. These results also lead to the conclusion that direct reduction of plastoquinone by FNR is negligible.

[Bioequivalence of phenylbutazone preparations following a single intramuscular administration]. / Bioäquivalenz von Phenylbutazon-Präparaten nach einmaliger intramuskulärer Applikation.

Bioequivalence was estimated in 6 resp. 7 male volunteers for two combination drugs of phenylbutazone (Neuro-Elmedal, Sigma Elmedal) after intramuscular administration using a monopreparation as a standard. Plasma levels of phenylbutazone were assayed by high pressure liquid chromatography. With respect to rate and extent both combination drugs were identical to the mono drug.