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1.
Mem. Inst. Oswaldo Cruz ; 110(1): 114-124, 03/02/2015. tab
Article in English | LILACS | ID: lil-741621

ABSTRACT

This paper presents, from the perspective of technological development and production, the results of an investigation examining 61 clinical studies with vaccines conducted in Brazil between 1938-2013, with the participation of the Oswaldo Cruz Institute (IOC) and the Oswaldo Cruz Foundation (Fiocruz). These studies have been identified and reviewed according to criteria, such as the kind of vaccine (viral, bacterial, parasitic), their rationale, design and methodological strategies. The results indicate that IOC and Fiocruz have accumulated along this time significant knowledge and experience for the performance of studies in all clinical phases and are prepared for the development of new vaccines products and processes. We recommend national policy strategies to overcome existing regulatory and financing constraints.


Subject(s)
Animals , Animal Feed/adverse effects , Dietary Proteins/chemistry , Models, Biological , Proanthocyanidins/chemistry , Rumen/metabolism , Brassica rapa/chemistry , Chemical Precipitation , Dietary Proteins/metabolism , Fermentation , Fabaceae/adverse effects , Fabaceae/chemistry , Fruit/adverse effects , Fruit/chemistry , Molecular Structure , Molecular Weight , Osmolar Concentration , Plant Proteins/chemistry , Plant Proteins/metabolism , Proanthocyanidins/adverse effects , Proanthocyanidins/metabolism , Ruminants , Ribulose-Bisphosphate Carboxylase/chemistry , Ribulose-Bisphosphate Carboxylase/metabolism , Rumen/microbiology , Solubility , Stereoisomerism , Serum Albumin, Bovine/chemistry , Serum Albumin, Bovine/metabolism
2.
Biol. Res ; 40(2): 137-153, 2007. graf, tab
Article in English | LILACS | ID: lil-468185

ABSTRACT

We quantified the ozone impact on levels of Zea mays L. cv. Chambord mRNAs encoding C4-phosphoenolpyruvate carboxylase (C4-PEPc), ribulose-l,5-bisphosphate carboxylase/oxygenase small and large subunits (Rubisco-SSU and Rubisco-LSU, respectively) and Rubisco activase (RCA) using real-time RT-PCR. Foliar pigment content, PEPc and Rubisco protein amounts were simultaneously determined. Two experiments were performed to study the ozone response of the 5th and the 10th leaf. For each experiment, three ozone concentrations were tested in open-top chambers: non-filtered air (NF, control) and non-filtered air containing 40 (+40) and 80 nL L-1 (+80) ozone. Regarding the 5th leaf, +40 atmosphere induced a loss in pigmentation, PEPc and Rubisco activase mRNAs. However, it was unable to notably depress carboxylase protein amounts and mRNAs encoding Rubisco. Except for Rubisco mRNAs, all other measured parameters from 5th leaf were depressed by +80 atmosphere. Regarding the 10th leaf, +40 atmosphere increased photosynthetic pigments and transcripts encoding Rubisco and Rubisco activase. Rubisco and PEPc protein amounts were not drastically changed, even if they tended to be increased. Level of C4-PEPc mRNA remained almost stable. In response to +80 atmosphere, pigments and transcripts encoding PEPc were notably decreased. Rubisco and PEPc protein amounts also declined to a lesser extent. Conversely, the level of transcripts encoding both Rubisco subunits and Rubisco activase that were not consistently disturbed tended to be slightly augmented. So, the present study suggests that maize leaves can respond differentially to a similar ozone stress.


Subject(s)
Ozone/pharmacology , Phosphoenolpyruvate Carboxylase/metabolism , Ribulose-Bisphosphate Carboxylase/metabolism , Zea mays/drug effects , Zea mays/enzymology , Phosphoenolpyruvate Carboxylase/drug effects , Plant Leaves/drug effects , Plant Leaves/enzymology , Plant Proteins/metabolism , Reverse Transcriptase Polymerase Chain Reaction , RNA, Messenger/drug effects , RNA, Plant/drug effects , Ribulose-Bisphosphate Carboxylase/drug effects , Zea mays/genetics
3.
J Environ Biol ; 2004 Jul; 25(3): 287-90
Article in English | IMSEAR | ID: sea-113677

ABSTRACT

Plants fumigated with 40ppbv, 80ppbv and 120ppbv concentrations of O3 exhibited significant reduction in total chlorophyll content, RuBP carboxylase activity and net photosynthesis. The reduction in total chlorophyll activity ranged from 12 to 36% in Bauhinia variegata, 11 to 35% in Ficus infectoria and 3 to 26% in Pongamia pinnata on fumigation with O3, while the RuBP carboxylase activity was reduced by 10 to 32% in Bauhinia variegata, 10 to 23% in Ficus infectoria and 9 to 15% in Pongamia pinnata. The net photosynthesis was also reduced by 6 to 26% in B. variegata, 16 to 39% in F. infectoria and 7 to 31% in P. pinnata on fumigation with 03. The relative higher sensitivity of tropical trees to O3 suggests that the ambient air quality standards in tropical tree areas need to be stringent to prevent vegetation from air pollution.


Subject(s)
Air Pollutants/toxicity , Bauhinia/drug effects , Chlorophyll/analysis , Dose-Response Relationship, Drug , Environmental Pollution , Ficus/drug effects , Millettia/drug effects , Ozone/toxicity , Photosynthesis/drug effects , Plant Transpiration/drug effects , Ribulose-Bisphosphate Carboxylase/metabolism , Trees/drug effects
4.
Indian J Exp Biol ; 2001 Nov; 39(11): 1191-3
Article in English | IMSEAR | ID: sea-56395

ABSTRACT

Two wheat varieties, T. durum (HD 4502) and T. aestivum (Kalyansona) were examined for photosynthesis rate and contents of sugars and rubisco protein in the flag leaf, at forenoon and afternoon at anthesis stage. A decrease in photosynthesis rate was observed in the afternoon compared to forenoon in both the varieties and was associated with an increase in non-reducing sugars and a decrease in rubisco content in the leaves.


Subject(s)
Carbohydrate Metabolism , Photosynthesis , Plant Leaves/metabolism , Ribulose-Bisphosphate Carboxylase/metabolism , Triticum/metabolism
5.
Indian J Exp Biol ; 2000 Aug; 38(8): 841-4
Article in English | IMSEAR | ID: sea-56897

ABSTRACT

Photosynthetic characteristics in kenaf (Hibiscus cannabinus L.), a C3 plant, were compared with Abelmoschus esculentus (L.) Moench, another member of Malvaceae. Kenaf leaves exhibited significantly higher rate of photosynthesis (40 mg CO2 dm(-2) hr(-1)) which was 24.6 mg dm(-2) hr(-1) in A. esculentus. Rate of photo and dark respiration was similar in both the species. Kenaf leaf photosynthesis had a higher optimum temperature (32 degrees C) than that of A. esculentus (26 degrees C). Photosynthesis in kenaf leaves required higher saturation irradiance (1,600 micromole m(-2) sec(-1)). There was a significant correlation between photosynthetic rate and biomass yield in these species. The primary product of photosynthesis after 5 seconds of 14C-assimilation was 3-PGA in both the species. The kinetic properties of RuBP carboxylase/oxygenase were determined in the leaf extracts. Higher carboxylase activities were recorded with kenaf leaf extracts (245 pmole mg chl(-1) hr(-1)). Km (CO2) for kenaf leaf carboxylase was significantly lower (7.8 microM) than A. esculentus (13.5 microM) and corresponding difference in Vmax values of carboxylase was recorded between the two species. The kinetic characteristics of oxygenase were similar in both the extracts. These results indicated the variation in carboxylase activity and its kinetic characteristics reflected a significant difference in CO2 assimilation in C3 plants.


Subject(s)
Hibiscus/enzymology , Kinetics , Photosynthesis , Ribulose-Bisphosphate Carboxylase/metabolism
6.
Indian J Biochem Biophys ; 1994 Aug; 31(4): 215-20
Article in English | IMSEAR | ID: sea-27990

ABSTRACT

Calvin cycle multienzyme complex, consisting of phosphoriboisomerase, phosphoribulokinase and ribulose-1,5-bisphosphate carboxylase (Rubisco), shows ribose-5-phosphate + ATP dependent CO2 fixation activity with a small but discernible lag. Transient time analysis showed that the lag at pH 7 was independent of multienzyme concentration and was significantly lower than the expected transient time calculated from Km and Vmax of the individual enzymes, indicative of channeling of the intermediates in the enzyme complex. Channeling of ribulose-1,5-bisphosphate was found to offer a catalytic advantage to Rubisco. Rubisco shows a decrease in activity during catalysis in ribulose-1,5-bisphosphate dependent CO2 fixation reaction, due to the formation of the catalytic inhibitor. Such a decrease of Rubisco activity was not observed in ribose-5-phosphate + ATP dependent CO2 fixation reaction and the catalytic inhibitor was also not detected. These results suggested that the intermediates are channeled in the complex and channeling offers a catalytic facilitation to Rubisco.


Subject(s)
Aldose-Ketose Isomerases , Carbohydrate Epimerases/metabolism , Catalysis , Multienzyme Complexes/metabolism , Phosphotransferases (Alcohol Group Acceptor)/metabolism , Plant Leaves , Ribulose-Bisphosphate Carboxylase/metabolism , Spinacia oleracea
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