| 1. |
- Bjorck, S, et al.
(författare)
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Synchronized terrestrial-atmospheric deglacial records around the North Atlantic
- 1996
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Ingår i: SCIENCE. - : AMER ASSOC ADVANCEMENT SCIENCE. - 0036-8075. ; 274:5290, s. 1155-1160
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Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)abstract
- On the basis of synchronization of three carbon-14 (C-14)-dated lacustrine sequences from Sweden With tree ring and ice core records, the absolute age of the Younger Dryas-Preboreal climatic shift was determined to be 11,450 to 11,390 +/- 80 years before
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| 2. |
- Björck, S., et al.
(författare)
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Synchronized terrestrial-atmospheric deglacial records around the North Atlantic.
- 1996
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Ingår i: Science. - : American Association for the Advancement of Science (AAAS). - 0036-8075 .- 1095-9203. ; 274:5290, s. 1155-1160
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Tidskriftsartikel (refereegranskat)abstract
- On the basis of synchronization of three carbon-14 (C-14)-dated lacustrine sequences from Sweden With tree ring and ice core records, the absolute age of the Younger Dryas-Preboreal climatic shift was determined to be 11,450 to 11,390 +/- 80 years before the present. A 150-year-long cooling in the early Preboreal, associated with rising Delta(14)C values, is evident in all records and indicates an ocean ventilation change. This cooling is similar to earlier deglacial coolings, and box-model calculations suggest that they all may have been the result of increased freshwater forcing that inhibited the strength of the North Atlantic heat conveyor, although the Younger Dryas may have begun as an anomalous meltwater event.
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| 3. |
- Hurry, Vaughan, 1960-, et al.
(författare)
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Mitochondria contribute to increased photosynthetic capacity of leaves of winter rye (Secale-Cereale L) following cold-hardening
- 1995
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Ingår i: Plant, Cell and Environment. - 0140-7791 .- 1365-3040. ; 18:1, s. 69-76
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Tidskriftsartikel (refereegranskat)abstract
- Cold-hardening of winter rye (Secale cereale L. cv. Musketeer) increased dark respiration from -2.2 to -3.9 mu mol O-2 m(-2)s(-1) and doubled light- and CO2-saturated photosynthesis at 20 degrees C from 18.1 to 37.0 mu mol O-2 m(-2) s(-1). We added oligomycin at a concentration that specifically inhibits oxidative phosphorylation to see whether the observed increase in dark respiration reflected an increase in respiration in the light, and whether this contributed to the enhanced photosynthesis of cold-hardened leaves, Oligomycin inhibited light- and CO2-saturated rates of photosynthesis in non-hardened and cold-hardened leaves by 14 and 25%, respectively, and decreased photochemical quenching of chlorophyll a fluorescence to a greater degree in cold-hardened than in non-hardened leaves, These data indicate an increase both in the rate of respiration in the light, and in the importance of respiration to photosynthesis following cold-hardening, Analysis of metabolite pools indicated that oligomycin inhibited photosynthesis by limiting regeneration of ribulose-1,5-bisphosphate, This limitation was particularly severe in cold-hardened leaves, and the resulting low 3-phosphoglycerate pools led to a feed-forward inhibition of sucrose-phosphate synthase activity, Thus, it does not appear that oxidative phosphorylation supports the increase in photosynthetic O-2 evolution following cold-hardening by increasing the availability of cytosolic ATP, The data instead support the hypothesis that the mitochondria function in the light by using the reducing equivalents generated by nan-cyclic photosynthetic electron transport.
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| 4. |
- Kromer, S, et al.
(författare)
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Regulation of the supply of cytosolic oxaloacetate for mitochondrial metabolism via phospho enolpyruvate carboxylase in barley leaf protoplasts .1. The effect of covalent modification on PEPC activity, pH response, and kinetic properties
- 1996
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Ingår i: Biochimica et Biophysica Acta - General Subjects. - 0304-4165 .- 1872-8006. ; 1289:3, s. 343-350
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Tidskriftsartikel (refereegranskat)abstract
- The regulation of the supply of oxaloacetate (OAA) for mitochondrial metabolism via phosphoenolpyruvate carboxylase (PEPC) by covalent modification is studied in barley (Hordeum vulgare L.) leaf protoplasts in light or darkness as well as under photorespiratory or non-photorespiratory conditions. Extracts for studies on in vivo PEPC phosphorylation were prepared from barley leaf protoplasts by rapid filtration, fractionating the cell within less than 1 s. Measurements of in vitro PEPC activity were performed on samples quickly frozen in liquid nitrogen to break the cell and stop metabolism and thus preserve the in vivo activation state. The relative PEPC phosphorylation state increased upon illumination and decreased upon redarkening under photorespiratory and non-photorespiratory conditions. PEPC activity measured in the presence of malate (3 mM) under photorespiratory conditions showed the same response indicating that a light-induced increase in PEPC activity and decrease in malate sensitivity is caused by an increased phosphorylation level of the PEPC protein. PEPC activity was pH dependent. At the physiological cytosolic pH, activity was suboptimal, but most sensitive towards malate inhibition and glucose 6-phosphate stimulation. The presence of malate increased the sensitivity of PEPC activity towards pH changes. The response of PEPC activity to changing pH was not affected by changes in the activation state of the enzyme. The K-m (phosphoenolpyruvate, PEP) is about 1 mM. Upon illumination the K-m (PEP) decrease significantly. V-max was unaffected by the light treatment. The presence of physiological concentrations of glucose 6-phosphate decreased K-m (PEP) 5- to 10-fold and increased V-max by about 35%. The effect of glucose 6-phosphate was strongest (up to 7-fold) at subsaturating PEP concentrations stimulating PEPC activity to nearly maximal rates. The results show that an increase in PEPC phosphorylation state causes an increase in PEPC activity as well as in substrate affinity leading to an increased production of OAA in the light.
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| 5. |
- Kromer, S, et al.
(författare)
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Regulation of the supply of oxaloacetate for mitochondrial metabolism via phospho enolpyruvate carboxylase in barley leaf protoplasts .2. Effects of metabolites on PEPC activity at different activation states of the protein
- 1996
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Ingår i: Biochimica et Biophysica Acta - General Subjects. - 0304-4165 .- 1872-8006. ; 1289:3, s. 351-361
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Tidskriftsartikel (refereegranskat)abstract
- The regulation of the supply of oxaloacetate (OAA) for mitochondrial metabolism via phosphoenolpyruvate carboxylase (PEPC) by metabolites is studied in barley (Hordeum vulgare L.) leaf protoplasts in light or darkness as well as under photorespiratory or non-photorespiratory conditions. Measurements on PEPC activity were performed on samples quickly frozen in liquid nitrogen to break the cell and stop metabolism and thus preserve the in vivo activation state. Glycine, serine, pyruvate, acetyl-CoA, glycolate, fructose 1,6-bisphosphate, fructose 2,6-bisphosphate and ADP had no significant effect on PEPC activity. Malate, aspartate and glutamate were strong inhibitors of PEPC activity decreasing the activity more in light versus darkness. However, at the physiological cytosolic concentration of these metabolites under the respective conditions, inhibition of PEPC activity was about the same with the exception of aspartate which inhibits more under non-photorespiratory than under photorespiratory conditions. 2-Oxoglutarate and glyoxylate decreased PEPC activity by 20 to 40% in the range of its physiological cytosolic concentration. Inhibition by physiological cytosolic concentrations of glutamine was limited. Glucose B-phosphate, fructose B-phosphate, 3-phosphoglycerate, dihydroxyacetonphosphate and P-i stimulated PEPC activity significantly in their physiological cytosolic concentration range. Physiological cytosolic concentrations of glucose 6-phosphate and fructose 6-phosphate activated PEPC activity to about the same extent under all conditions applied, while 3-phosphoglycerate and dihydroxyacetonphosphate stimulating Stronger under non-photorespiratory versus photorespiratory conditions. Moreover, dihydroxyacetonphosphate stimulated PEPC activity more in light versus darkness under non-photorespiratory conditions. P-i activation of PEPC activity decreases in light versus darkness under non-photorespiratory conditions. Stimulation of PEPC activity by citrate in its physiological concentration range is limited. Glucose 1-phosphate and AMP activated PEPC activity only at concentrations higher than their physiological levels in the cytosol. Determinations of PEPC activity in the presence of different malate/glucose 6-phosphate ratios revealed that glucose 6-phosphate totally relieved the inhibitory effect of malate. The regulatory properties of PEPC activity will be discussed in relation to its functions in C-3 plants.
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