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| 2. |
- Christensen, Torben, et al.
(författare)
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Trace gas exchange in a high-arctic valley 1. Variations in CO2 and CH4 flux between tundra vegetation types
- 2000
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Ingår i: Global Biogeochemical Cycles. - 0886-6236. ; 14:3, s. 701-714
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Tidskriftsartikel (refereegranskat)abstract
- Ecosystem exchanges of CO2 and CH4 were studied by chamber techniques in five different vegetation types in a high arctic valley at Zackenberg, NE Greenland. The vegetation types were categorized as Cassiope heath, hummocky fen, continuous fen, grass land and Salix arctica snowbed. Integrated daytime fluxes for the different vegetation types of the valley showed that the fen areas and the grassland, were significant sources of CH4 with a mean efflux of 6.3 mg CH4 m(-2) h(-1) and sinks for CO2, with almost -170 mg CO2 m(-2) hr(-1). The heath and snowbed areas had much lower carbon sequestration rates of about -25 mg CO2 m(-2) hr(-1) and were also sinks for CH4. Methane emissions from the valley dominated in the hummocky fens. Computation of area integrated mean daytime flux values across all vegetation types of the entire valley bottom revealed that it was a sink of CO2 in the order of -96+/-33 mg CO2 m-2 hr-1 and a source of 1.9+/-0.7 m(-2) CH4 m(-2) hr(-1). These values were in accordance with eddy correlation measurements reported elsewhere in this issue and reflect a high-carbon exchange despite the high arctic location. In the fens, where the water table was at or above the soil surface, methane emissions increased with net ecosystem CO2 flux. In places with the water table below the soil surface, such as particularly in the hummocky parts of the fen, oxidation tended to become the dominant controlling factor on methane efflux.
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| 3. |
- Fredriksson, A., et al.
(författare)
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Labeling of human C-peptide by conjugation with N-succinimidyl-4- F-18 fluorobenzoate
- 2001
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Ingår i: Journal of labelled compounds & radiopharmaceuticals. - : Wiley. - 0362-4803 .- 1099-1344. ; 44:7, s. 509-519
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Tidskriftsartikel (refereegranskat)abstract
- We have labeled proinsulin connecting peptide (C-peptide) with fluorine-18 (t(1/2) = 109.7min) in order to perform in vivo biodistribution and pharmacokinetic studies with position emission tomography (PET). This study reports the optimization of the conjugation labeling in the N-terminal with N-succinimidyl-4-[F-18]fluorobenzoate ([F-18]SFB). In preparative runs N-4-[F-18]fluorobenzoyl-C-peptide ([F-18]FB-C-peptide) was produced in 8-12% decay-corrected yields, counted from resolubilized [F-18]F-, in less than 5h. The specific radioactivity of [F-18]FB-C-peptide, determined using ELISA for one of the preparations, was around 70 GBq/mu mol at end of synthesis.
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| 4. |
- Johansson, Maria U, et al.
(författare)
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Structure, specificity, and mode of interaction for bacterial albumin-binding modules.
- 2002
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Ingår i: Journal of Biological Chemistry. - 1083-351X .- 0021-9258. ; 277:10, s. 8114-8120
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Tidskriftsartikel (refereegranskat)abstract
- We have determined the solution structure of an albumin binding domain of protein G, a surface protein of group C and G streptococci. We find that it folds into a left handed three-helix bundle similar to the albumin binding domain of protein PAB from Peptostreptococcus magnus. The two domains share 59% sequence identity, are thermally very stable, and bind to the same site on human serum albumin. The albumin binding site, the first determined for this structural motif known as the GA module, comprises residues spanning the first loop to the beginning of the third helix and includes the most conserved region of GA modules. The two GA modules have different affinities for albumin from different species, and their albumin binding patterns correspond directly to the host specificity of C/G streptococci and P. magnus, respectively. These studies of the evolution, structure, and binding properties of the GA module emphasize the power of bacterial adaptation and underline ecological and medical problems connected with the use of antibiotics.
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| 7. |
- Jonasson, P., et al.
(författare)
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Integrated bioprocess for production of human proinsulin C-peptide via heat release of an intracellular heptameric fusion protein
- 2000
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Ingår i: Journal of Biotechnology. - 0168-1656 .- 1873-4863. ; 76:03-feb, s. 215-226
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Tidskriftsartikel (refereegranskat)abstract
- An integrated bioprocess has been developed suitable for production of recombinant peptides using a gene multimerization strategy and site-specific cleavage of the resulting gene product. The process has been used for production in E. coli of the human proinsulin C-peptide via a fusion protein BB-C7 containing seven copies of the 31-residues C-peptide monomer. The fusion protein BB-C7 was expressed at high level, 1.8 g l(-1), as a soluble gene product in the cytoplasm. A heat treatment procedure efficiently released the BB-C7 fusion protein into the culture medium. This step also served as an initial purification step by precipitating the majority of the host cell proteins, resulting in a 70% purity of the BB-C7 fusion protein. Following cationic polyelectrolyte precipitation of the nucleic acids and anion exchange chromatography, native C-peptide monomers were obtained by enzymatic cleavage at flanking arginine residues. The released C-peptide material was further purified by reversed-phase chromatography and size exclusion chromatography. The overall yield of native C-peptide at a purity exceeding 99% was 400 mg l(-1) culture, corresponding to an overall recovery of 56%. The suitability of this process also for the production of other recombinant proteins is discussed.
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