Search results for "thermophilic"
showing 6 items of 16 documents
Interactions between Streptococcus thermophilus and thermophilic lactobacilli strongly affect its growth during pressing of swiss-type cheeses
2007
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Habitat effect on distribution and feeding of Ophidiaster ophidianus (Lmk.) (Asteroidea)
2016
The purple starfish Ophidiaster ophidianus is an Atlanto-Mediterranean starfish protected under the EU’s Habitats Directive. Despite the wide distribution and the current range expansion of this warm affinity species in the northern Mediterranean areas, nothing is known about its diet. Using field observations and carbon (δ13C) and nitrogen (δ15N) stable isotopes, we explored possible changes in density and diet of O. ophidianus in relation to two different Mediterranean habitats: the coralline barren and the macro algae forest. Data were collected at the Marine Protected Area of Ustica Island (Southern Tyrrhenian Sea) from June to September 2009. Starfish density was not affected by the ha…
Photoaffinity cross-linking of F1ATPase from the thermophilic bacterium PS3 by 3′-arylazido-β-alanyl-2-azido ATP
1989
AbstractThe photoactivatable bifunctional 3′-arylazido-β-alanyl-2-azido ATP (2,3′-DiN3ATP) has been applied to study the localization of the nucleotide-binding sites of coupling factor 1 (F1ATPase, TF1) from the thermophilic bacterium PS3 by photoaffinity cross-linking. UV irradiation of TF1 in the presence of 2,3′-DiN3ATP results in the nucleotide-dependent formation of various higher molecular mass cross-links formed by two, three or even four α- and/or β-subunits. The differences observed upon photoaffinity cross-linking by the bifunctional 2-azido ATP or 8-azido ATP analog are discussed. They are probably due to the varied maximal distance between both azido groups, or to the different …
Photoaffinity labeling of the coupling factor 1 from the thermophilic bacterum PS3 by 8-azido ATP
1984
AbstractTo localize the nucleotide binding sites of the F1ATPase (TF1) from the thermophilic bacterium PS3 we have used 14C-labeled 8-azido ATP (8-N3ATP) as photoaffmity label. 8-N3ATP is hydrolyzed by the F,ATPase in the absence of ultraviolet light. Irradiation by ultraviolet light of the enzyme in the presence of 8-N3ATP results in reduction of ATPase activity and in preferential nucleotide specific labeling of the α subunits (0.8–0.9 mol 8-N3ATP/TF1,α:β = 4:1). Inactivation and labeling do not depend on the presence of Mg2+. Both effects decrease upon addition of various nucleotide di- or triphosphates.