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M Avron

Publications and source records attributed to M Avron.

At least 73 records · Page 4Linked to original sources
PubMed1974

Properties of phosphoribulokinase of whole chloroplasts.

The ability of intact spinach (Spinacia oleracea) chloroplast preparations to catalyze CO(2) fixation and photophosphorylation was examined. Under conditions optimal for CO(2) fixation, only poor photophosphorylation was observed. Conditions optimal for photophosphorylation were found to be highly inhibitory to the CO(2)-fixing capacity of the intact chloroplast preparation.A method for following the activity of phosphoribulokinase in the intact chloroplast preparation was developed, and conditions for optimal activity were defined. The enzyme was found to be activated 2- to 4-fold by preillumination with a half-time of less than 15 seconds. Activation was inhibited by magnesium ions and selectively by inhibitors of photosynthetic electron transport. We concluded that activation was due to the effect of a photoproduced reductant in a site preceding ferredoxin in the electron transport chain. The photoactivated state of the enzyme decayed in the dark with a half-time of about 8 minutes.

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PubMed1974

Carbon dioxide fixation in the light and in the dark by isolated spinach chloroplasts.

Factors affecting CO(2) fixation in the spinach (Spinacia oleracea) chloroplast were investigated. Free magnesium ions are shown to be highly inhibitory for photosynthetic CO(2) fixation in isolated intact spinach chloroplasts. The pH optimum for CO(2) fixation is about 8.5 but is dependent upon the reaction medium. Conditions are defined under which chloroplasts illuminated in the absence of CO(2) accumulate ribulose 1,5-diphosphate, and fix CO(2) in a subsequent dark period when high magnesium ion concentrations are provided. The regulation of photosynthetic CO(2) assimilation by these factors is discussed.

Journal Article↗
PubMed1974

Isolation, 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, respectively. The enzyme has a very narrow substrate specificity and will not catalyze the reduction of glyceraldehyde or dihydroxyacetone phosphate. It is suggested that this enzyme functions physiologically as a dihydroxyacetone reductase in the path of glycerol synthesis and accumulation in Dunaliella.

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PubMed1973

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 varied accordingly, reaching its new osmotic equilibrium after about 90 minutes. Since no leakage of intracellular glycerol was observed above 0.6 m NaCl, these alterations in glycerol content are interpreted as due to metabolic formation and degradation of intracellular glycerol. The above results indicate the existence of a new type of algal osmoregulation, in which the osmotic balance depends on the synthesis or degradation of intracellular glycerol in response to the external salt concentration.

Journal Article↗
PubMed1972

Photosynthetic Activities of the Halophilic Alga Dunaliella parva.

Dunaliella parva, a unicellular halophilic alga, was found to evolve oxygen photosynthetically only in the presence of a high osmolar concentration. Cell free preparations were obtained by placing the cells in a medium of low osmolarity. The fragments obtained showed a high photoreducing and photophosphorylating activity except for their inability to catalyze all ferredoxin dependent photoreactions. Placing the cells in a medium of intermediate osmolarity produced a "chloroplast" preparation which maintained some capacity for O(2) evolution and CO(2) fixation, while possessing the ability to catalyze the photoinduced reduction of ferricyanide. Enzymic and photosynthetic reactions of cell-free preparations from D. parva were inhibited, rather than stimulated, by the salt concentration optimal for growth. These results were interpreted as indicating the existence of a steep NaCl gradient in vivo between the medium and the cell compartments which are not permeable to salt.

Journal Article↗
PubMed1972

Is nicotinamide adenine dinucleotide phosphate an obligatory intermediate in photosynthesis?

The site of action of the inhibitors disalicylidenepropanediamine and pyrophosphate was more closely defined as acting on ferredoxin. Three inhibitors which act on the electron transport path between ferredoxin and NADP: disalicylidenepropanediamine, pyrophosphate, and phosphoadenosinediphosphate ribose, had no effect on photosynthesis in cell free preparations of Dunaliela parva at concentrations which completely inhibited the enzymic activity on which each inhibitor acts. The addition of disalicylidenepropanediamine to dark-grown Euglena gracilis cells prevented the light-induced formation of NADP-dependent glyceraldehyde-3-phosphate dehydrogenase, but not of photosynthesis, chlorophyll synthesis, or NAD-dependent glyceraldehyde-3-phosphate dehydrogenase.The above results are interpreted as indicating that, at least under some conditions, a reduced product of photosystem I preceding ferredoxin in the electron transport path can serve as the reductant of CO(2) in photosynthesis.

Journal Article↗
PubMed1972

Enhancement.

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Chloroplasts↗