Preferencje help
Widoczny [Schowaj] Abstrakt
Liczba wyników

Znaleziono wyników: 11

Liczba wyników na stronie
Pierwsza strona wyników Pięć stron wyników wstecz Poprzednia strona wyników Strona / 1 Następna strona wyników Pięć stron wyników wprzód Ostatnia strona wyników

Wyniki wyszukiwania

help Sortuj według:

help Ogranicz wyniki do:
Pierwsza strona wyników Pięć stron wyników wstecz Poprzednia strona wyników Strona / 1 Następna strona wyników Pięć stron wyników wprzód Ostatnia strona wyników
In plants, vacuolar invertase (β-fructofuranosidase, EC 3.2.1.26) is known to play as a key modulator for hexose accumulation and cell expansion. In this study, two cDNA clones (2,013 and 1,945 bp, with 99 % sequence identity) encoding vacuolar invertase isoforms were isolated from a commercially important Indian potato cultivar, Kufri Chipsona-1 by RT-PCR. The corresponding predicted proteins consisted of 635 amino acids (designated as KC-VIN1, lacking a few amino acids at N-terminus) and 639 amino acids (designated as KC-VIN2), respectively. They showed 99 % identity, and found to vary at several locations with mostly non-conservative substitutions. Multiple sequence alignment of vacuolar invertase homologs covering four Solanaceae family members revealed some notable distinguishing sequence features (signature-type sequences). A consensus sequence was predicted using 45 vacuolar invertase sequences from 27 taxonomically different plant species, and a phylogenetic tree was generated to know the evolutionary relation between them. Hydrophobic characters were predicted, and compared in different plant species. All these data are presented in a comprehensive manner which were not documented in the earlier reports. As a preliminary study, vacuolar invertase expression patterns in the tubers of some Indian potato cultivars were analyzed by semi-quantitative RT-PCR and extractable enzyme assay. In all the potato cultivars, the overall expression level of invertase was found to be considerably higher after storage at low temperature as compared to the freshly harvested tubers.
Sucrose-phosphate synthase (SPS, EC 2.4.1.14) refers to a key enzyme in sucrose biosynthesis in both photosynthetic and nonphotosynthetic tissues of plants. It is encoded by different gene families. SPS exists in multiple forms which show differential distributions and functional specializations in the plant tissues. SPS activity is highly regulated by hierarchy of mechanisms including transcriptional control. Here, we report an isolation of a cDNA clone (3,591 bp) encoding full-length SPS A form consisting of 1,054 amino acids (designated KC-SPS1) from a commercially important Indian potato (Solanum tuberosum L.) cultivar, Kufri Chipsona-1 by RT-PCR approach from tuber total RNA. KC-SPS1 shared 99 % sequence identity with 1,053-amino acid SPS from potato cv. Desiree. Apart from some prominent amino acid substitutions, one extra Met residue at position 235 made KC-SPS1 a distinct member of SPS A family in potato. Full-length SPS sequences from taxonomically different plant species were used in making a phylogenetic tree which showed both evolutionary relatedness, and also their grouping into different SPS families. Hydropathy characters and secondary structures were predicted in various SPS forms. Sequence analyses and comparison of the SPS sequences from the Solanaceae family members revealed many distinct features within and between the SPS gene families which were not documented earlier. SPS A form-specific expression patterns were studied in the leaves and tubers of different potato cultivars based on semi-quantitative RT-PCR and protein blot analyses. SPS activities particularly in the cold-stored tubers were probably due to altered kinetic properties. This report would be useful for in-depth studies on various SPS isoforms in potato and other Solanaceae family members.
5
Artykuł dostępny w postaci pełnego tekstu - kliknij by otworzyć plik
Content available

Role of Nanoplanktons in Marine food-webs

71%
Nanoplanktons are ubiquitous protozoan zooplankton in a size range of 2 to 20 μm, play key ecological roles in aquatic ecosystems. Heterotrophic nanoflagellates are distributed through the continental shelf and margin area of the oceans as well as deep-sea. These organisms contribute significantly to the total living biomass within these systems, serve as the major top–down control on bacterial assemblages, and are an important source of mortality for microalgae and other heterotrophic nanoflagellates. From many recent studies, it is generally accepted that HNF is one of the most important bacterial consumers. They also function as important remineralizers of organic matter and nutrients in aquatic systems. In accordance with these important ecological roles, heterotrophic nanoflagellates have been the subject of considerable study both in the field and laboratory.
Methane is a most important greenhouse gas for planetary heating and it’s produced by methanogenic microorganisms as a metabolic byproduct and creates climate change. Methanogens are ancient organisms on earth found in anaerobic environments and methane is a key greenhouse gas concerned with methanogens. Therefore here is intense interest to writing this paper. A number of experiments have already conducted to study the methanogens in various environments such as rumen and intestinal system of animals, fresh water and marine sediments, swamps and marshes, hot springs, sludge digesters, and within anaerobic protozoa which utilize carbon dioxide in the presence of hydrogen and produce methane. The diversity of methanogens, belong to the domain Archaea and get involved in biological production of methane that catalyzes the degradation of organic compound as a part of global carbon cycle called methanogenesis. Majorly in this article we summaries the diversity of methanogens and their impact on global warming.
Pierwsza strona wyników Pięć stron wyników wstecz Poprzednia strona wyników Strona / 1 Następna strona wyników Pięć stron wyników wprzód Ostatnia strona wyników
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.