Natural transformation of the filamentous cyanobacterium Phormidium lacuna
نویسندگان
چکیده
منابع مشابه
Cytochrome c Oxidase of the Cyanobacterium Phormidium foveolarum
Phormidium foveolarum was grown with nitrate or ammonia as nitrogen source. With ammonia present respiration increased by a factor of 4 due to increase of cytochrome c oxidase. The inhibition of respiration by cyanide was measured during the growth period, indicating that only one terminal oxidase is present in Phormidium foveolarum . Cytochrome c oxidase from ammoniagrown filaments was solubil...
متن کاملCharacterization of aspartate aminotransferase from the cyanobacterium Phormidium lapideum.
Aspartate aminotransferase (AspAT) was purified to homogeneity from cell extracts of the non-N2-fixing cyanobacterium Phormidium lapideum. The NH2-terminal sequence of 25 amino acid residues was different from the sequences of the subfamily Ialpha of AspATs from eukaryotes and Escherichia coli, but it was similar to sequences of the subfamily Igamma of AspATs from archaebacteria and eubacteria....
متن کاملStudies on a toxin produced by the cyanobacterium Phormidium persicinum.
As part of an on-going project to detect extracellular algal compounds of potential medicinal value aqueous culture supernatants and methanolic cell extracts of randomly selected algae were screened for the presence of bioactive compounds using electrically stimulated guineapig ileum preparations[l] and a brine shrimp assay[2]. Bioactive compounds were detected in the methanolic extract of the ...
متن کاملCrystal Structure of Allophycocyanin from Marine Cyanobacterium Phormidium sp. A09DM
Isolated phycobilisome (PBS) sub-assemblies have been widely subjected to X-ray crystallography analysis to obtain greater insights into the structure-function relationship of this light harvesting complex. Allophycocyanin (APC) is the phycobiliprotein always found in the PBS core complex. Phycocyanobilin (PCB) chromophores, covalently bound to conserved Cys residues of α- and β- subunits of AP...
متن کاملComposition of the ferredoxin-nitrite reductase from the cyanobacterium Phormidium laminosum.
Kidneys flush-stored with M C were compared with those in U W for 2 4 h and 48 h. At both 24 h and 48 h of storage, UW-stored organs produced si nificantly more glucose than those in MC. T h e uptake of "!I-PAH did not differ significantly between the two solutions. U W was subsequently modified, replacing raffinose with mannitol (solution A), lactobionate with citric acid (solution B), and sod...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: PLOS ONE
سال: 2020
ISSN: 1932-6203
DOI: 10.1371/journal.pone.0234440