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2. Co z raněnovověkých textů vydávat? A jak?
- Creator:
- Linka, Jan
- Format:
- Type:
- model:internalpart and TEXT
- Language:
- Czech
- Rights:
- http://creativecommons.org/licenses/by-nc-sa/4.0/ and policy:public
3. Contrasting changes of photosystem 2 efficiency in Arabidopsis xanthophyll mutants at room or low temperature under high irradiance stress
- Creator:
- Peng, Chang-Lian and Gilmore, A. M.
- Format:
- bez média and svazek
- Type:
- model:article and TEXT
- Subject:
- antheraxanthin, β-carotene, chlorophyll, fluorescence, light-harvesting complex, lutein, neoxanthin, violaxanthin, and zeaxanthin
- Language:
- Multiple languages
- Description:
- We compared the responses of wild type (WT) and three mutants including npq1 (lutein-replete and violaxanthin deepoxidase-deficient), lut2 (lutein-deficient), and lut2-npq1 (double mutant) to high irradiance (HI, 2 000 μmol m-2 s-1) at both low (LT, 5 °C) and room (25 °C) temperature. Xanthophyll-dependent energy dissipation was highest in the WT, followed by the lut2, npq1, and npq1-lut2. At 25 °C the relative stress tolerance expressed by Fv/Fm was consistent with the energy dissipation capacity for the first 2 h of treatment. After 3-4 h, the Fv/Fm levels in lut2 and npq1 converged. Under combined LT and HI the relative tolerance sequence was in contrast to the energy dissipation capacity being WT > npq1> lut2 > lut2-npq1. There were little or no significant change in the contents of xanthophylls and carotenes or the chlorophyll (Chl) a/b ratio in any of the materials. Thus lutein (L) substitution possibly alters the conformation/organisation of L binding proteins to enhance damage susceptibility under HI at LT. The enhanced vulnerability is not compensated for the energy dissipation capacity in the lut2 background at LT. and Chang-Lian Peng, A. M. Gilmore.
- Rights:
- http://creativecommons.org/licenses/by-nc-sa/4.0/ and policy:public
4. Novel agglutinin in the midgut of the tick Ixodes ricinus
- Creator:
- Uhlíř, Jan, Grubhoffer, Libor, and Volf, Petr
- Format:
- Type:
- model:internalpart and TEXT
- Subject:
- tick, Ixodes ricinus, midgut, and agglutinin
- Language:
- English
- Description:
- Haemagglutination activity (HA) was found and characterized in a midgut homogenate of Ixodes ricinus (L.). HA was induced by tick feeding; it was not detected in starved ticks. In a haemagglutination inhibition test, HA showed an affinity for some carbohydrates (N-acetyl-D-galactosamine, N-acetyl-D-glucosamine, rhamnose, and dulcit) and glycoconjugates (especially lipopolysaccharides). Midgut protein components of 37, 60, 65, and 73 kDa were identified by immunoblotting as potential structural subunits of the new agglutinin.
- Rights:
- http://creativecommons.org/licenses/by-nc-sa/4.0/ and policy:public