Photosynthetic Activities of the Halophilic Alga Dunaliella parva
نویسندگان
چکیده
منابع مشابه
The Role of Glycerol in the Osmotic Regulation of the Halophilic Alga Dunaliella parva.
Dunaliella parva, a green halophilic alga, was found to accumulate very large amounts of intracellular glycerol. Through measurements of the intracellular volume the internal concentration of glycerol was calculated and found to be around 2.1 m in cells cultured in 1.5 m NaCl. When the extracellular salt concentration of an algal suspension was increased or decreased, the intracellular glycerol...
متن کاملEffects of salts on the halophilic alga Dunaliella viridis.
Determinations of the salt sensitivity of enzymes extracted from the halophilic alga Dunaliella viridis revealed that pentose phosphate isomerase, ribulose diphosphate carboxylase, glucose-6-phosphate dehydrogenase, and phosphohexose isomerase were inhibited by NaCl concentrations far lower than that in the growth medium (3.75 m). The inhibition was reversible and was not prevented by preparing...
متن کاملThe Intracellular Distribution of Enzymes of the Glycerol Cycle in the Unicellular Alga Dunaliella parva
Glycerol is the main osmoticum of the unicellular green alga Dunaliella [1-4]. During the process of osmoregulation this solute has to be synthesized or degraded efficiently depending on the extent and direction of changes in the salinity of the external medium. Synthesis of glycerol starts from DHAP [5]. A glycerol-3-phosphate dehydrogenase (EC 1.1.1.8) reduces DHAP to glycerol-3-phosphate and...
متن کاملThe Plasma Membrane ATPase of Dunaliella parva
Plasma membrane Mg2+, Ca2+ ATPases were isolated from Dunaliella parva by differential centrifugation and subsequent sucrose gradient centrifugation and analyzed for their properties with special emphasis on ecophysiological requirements of this extremely salt-tolerant alga. Most properties (Vmaxand AfM-values, substrate specificity, vanadate and DES sensitivity, resistance against ouabain) ind...
متن کاملIsolation, Characterization, and Partial Purification of a Reduced Nicotinamide Adenine Dinucleotide Phosphate-dependent Dihydroxyacetone Reductase from the Halophilic Alga Dunaliella parva.
An NADP(+)-dependent dihydroxyacetone reductase, which catalyzes specifically the reduction of dihydroxyacetone to glycerol, has been isolated from the halophilic alga Dunaliella parva. The enzyme has been purified about 220-fold. It has a molecular weight of about 65,000 and is highly specific for NADPH. The pH optima for dihydroxyacetone reduction and for glycerol oxidation are 7.5 and 9.2, r...
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ژورنال
عنوان ژورنال: Plant Physiology
سال: 1972
ISSN: 0032-0889,1532-2548
DOI: 10.1104/pp.49.2.240