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2. Carbohydrate-binding specificities and physico-chemical properties of lectins in various tissue of phlebotominae sandflies

Creator:
Palánová, Lucie and Volf, Petr
Format:
print
Type:
model:internalpart and TEXT
Subject:
lectin, carbohydrates, sandfly, Phlebotomus, Lutzomyia, haemolymph, ovaries, midgut, and Leishmania
Language:
English
Description:
Physico-chemical properties and carbohydrate-binding specificity of hemagglutination activity (HA) were compared in tissue lysates and haemolymph of unfed and bloodied females of five sandfly species. Sandfly gut lectins were found to be heat-labile, sensitive to dithiotreitol treatment, freezing/thawing procedures and were affected by divalent cations. The pH optimum of HA ranged between 7.0-7.5. Specificity of gut HA of all species studied was directed towards aminosugars and some glycoconjugates, mainly lipopolysaccharide from Escherichia coli K-235, heparin and fetuin. Gut HA of Phlebotomus papatasi (Scopoli, 1786) was strongly inhibited by lipophosphoglycan (LPG) from Leishmania major promastigotes. In females, that took blood, the HA was higher but the carbohydrate-binding specificity remained the same; this suggests that the same lectin molecule was present, at different levels, both in unfed and fed flies. High HA was found in ovaries of fed females of Lutzomyia longipalpis (Lutz et Nieva, 1912), P. papatasi and P. duhoscqi Neveu-Lemaire, 1906. In P. papatasi and P. duboscqi the HA was present also in the haemolymph and head lysates of both fed and unfed females. Carbohydrate-binding specificity of HA present in these tissues was similar with the gut lectin.
Rights:
http://creativecommons.org/licenses/by-nc-sa/4.0/ and policy:public

4. Differential responses of photosynthetic parameters of pigeonpea and amaranth leaf discs to SO2

Creator:
Saraswathi, J. and Madhava Rao, K.V.
Format:
print
Type:
model:internalpart and TEXT
Subject:
Amaranthus paniculatus L., amino acids, Cajanus cajan (L.) Millsp., chlorophyll, CO2 fixation, phosphoenolpyruvate carboxylase, proteins, ribulose-1,5-bisphosphate carboxylase, SH- content, and sulphite oxidation
Language:
Multiple languages
Description:
The reduction in chlorophyll (Chl) and protein contents and the increase in amino acid content in leaf discs in response to aqueous SO2 exposure under continuous irradiance were more expressed in Amaranthus paniculatus (C4 plant) than in Cajanus cajan (C3 plant). The content of SH-compounds increased more in pigeonpea than in amaranth leaf discs in response to SO2. Aqueous SO2 exposure also reduced the CO2 fixation and ribulose-l,5-bisphosphate carboxylase (RuBPC) and phosphoenolpyruvate carboxylase (PEPC) activities in leaf discs of both plant species. The differences in sensitivity of these plants to SO2 were related to their conversion efficiency of SO2 to less toxic substances and sulphydryl compounds.
Rights:
http://creativecommons.org/licenses/by-nc-sa/4.0/ and policy:public

5. Diurnal changes in photosynthesis in relation to ribulose-1,5-bisphosphate carboxylase activíty and saccharides content in wheat leaves

Creator:
Sharma-Natu, P. and Ghildiyal, M.C.
Format:
print
Type:
model:internalpart and TEXT
Language:
Multiple languages
Description:
The diumal changes in leaf net photosynthetíc rate (P^) in two genotypes of wheat, T. aestivum (6x) cv. Sonalika and T. monococcum (2x) cv. G 1372, were analyzed in relatíon to stomatal (4) and mesophyll (/,J limitations of P^, ribulose-1,5- bisphosphate carboxylase (RuBPC) activity and saccharides content of the leaves. Pti decreased towards the aftemoon. The /„ was mostly contributing to the diumal decline in leaf at ear emergence stage. There was a decrease in activation statě of RuBPC in the aftemoon compared to forenoon. Associated with this a marked accumulation of saccharides in wheat leaf during the day was observed. Both the genotypes showed a more or less similar pattem of diumal changes in these parameters but differed in magnitude.
Rights:
http://creativecommons.org/licenses/by-nc-sa/4.0/ and policy:public

8. Mutation mechanism of chlorophyll-less barley mutant NYB

Creator:
Liu, Z.-L., Yuan, S., Liu, W.-J., Du, J.-B., Tian, W.-J., Luo, M.-H., and Lin, H.-H.
Format:
bez média and svazek
Type:
model:article and TEXT
Subject:
chlorophyll, fluorescence emission spectra, light-harvesting complex 2, Nanchong yellow barley (NYB), nucleotide sequences, photosystem 2, proteins, and protochlorophyllide oxidoreductase (POR)
Language:
Multiple languages
Description:
NYB is chlorophyll-less barley mutant, which is controlled by a recessive nuclear gene. The mutation mechanism is revealed. The activities of enzymes transforming 5-aminolevulinic acid into protochlorophyllide were the same in both NYB and the wild type (WT), but the activity of the protochlorophyllide oxidoreductase (POR) in WT was much higher than that of NYB. Most of the photosystem 2 apoproteins were present in both WT and NYB, suggesting that the capability of protein synthesis was probably fully preserved in the mutant. Thus chlorophyll (Chl) biosynthesis in NYB was hampered at conversion form protochlorophyllide (Pchlide) into chlorophyllide. The open reading frame of porB gene in NYB was inserted with a 95 bp fragment, which included a stop codon. The NYB mutant is a very useful material for studies of Chl biosynthesis, chloroplast signalling, and structure of light-harvesting POR-Pchlide complex (LHPP). and Z.-L. Liu ... [et al.].
Rights:
http://creativecommons.org/licenses/by-nc-sa/4.0/ and policy:public