Appendix

Peters, J. H.; Baumgarten, H.

doi:10.1007/978-3-642-74532-4_12

Cited by 13 publications

(18 citation statements)

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“…We will refer to the former as "random driving" and the latter as "linear driving". Random driving is the preferred model as it leads to SNe occurring mostly in the diffuse gas in the range of 0.01 < nH < 1cm −3 , which is consistent with more sophisticated simulations that include self-gravity and star formation (Gatto et al 2017;Peters et al 2017;Kim & Ostriker 2017). Linear driving is considered less realistic and serves as a comparison case.…”

Section: Sn-driven Multiphase Ismsupporting

confidence: 73%

“…Plasma drag has a negligible effect compared to direct collisions at nH,0 0.1cm −3 , but it becomes quite important in suppressing a sp,Si at nH,0 < 0.1cm −3 as the grain charge increases. On the other hand, betatron acceleration provides an efficient mechanism to enhance a sp,Si especially at nH,0 = 0.1cm −3 , which happens to be the typical density where SNe occur for solar-neighborhood conditions (Gatto et al 2017;Peters et al 2017;Kim & Ostriker 2017).…”

Section: The Grain-size Dependencementioning

confidence: 99%

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Thermal and non-thermal dust sputtering in hydrodynamical simulations of the multiphase interstellar medium

Zhukovska

Somerville

et al. 2019

Monthly Notices of the Royal Astronomical Society

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We study the destruction of interstellar dust via sputtering in supernova (SN) shocks using three-dimensional hydrodynamical simulations. With a novel numerical framework, we follow both sputtering and dust dynamics governed by direct collisions, plasma drag and betatron acceleration. Grain-grain collisions are not included and the grain-size distribution is assumed to be fixed. The amount of dust destroyed per SN is quantified for a broad range of ambient densities and fitting formulae are provided. Integrated over the grain-size distribution, nonthermal (inertial) sputtering dominates over thermal sputtering for typical ambient densities. We present the first simulations that explicitly follow dust sputtering within a turbulent multiphase interstellar medium. We find that the dust destruction timescales τ are 0.35 Gyr for silicate dust and 0.44 Gyr for carbon dust in solar neighborhood conditions. The SN environment has an important impact on τ . SNe that occur in preexisting bubbles destroy less dust as the destruction is limited by the amount of dust in the shocked gas. This makes τ about 2.5 times longer than the estimate based on results from a single SN explosion. We investigate the evolution of the dust-to-gas mass ratio (DGR), and find that a spatial inhomogeneity of ∼ 14% develops for scales below 10 pc. It locally correlates positively with gas density but negatively with gas temperature even in the exterior of the bubbles due to incomplete gas mixing. This leads to a ∼ 30% lower DGR in the volume filling warm gas compared to that in the dense clouds.

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Section: Sn-driven Multiphase Ismsupporting

confidence: 73%

Section: The Grain-size Dependencementioning

confidence: 99%

Thermal and non-thermal dust sputtering in hydrodynamical simulations of the multiphase interstellar medium

Zhukovska

Somerville

et al. 2019

Monthly Notices of the Royal Astronomical Society

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“…Spleen cells of mice were fused with X63-Ag8.653 myeloma cells. Fusion was done as described (21). After fusion, cells were plated in 200 wells of 24-well hybridoma plates (Greiner) in RPMI 1640 supplemented with 10% fetal calf serum, penicillin, streptomycine, 100 M hypoxanthine, 0.4 M aminopterin, 16 M thymidine (Boehringer-Mannheim).…”

Section: Materials-cellmentioning

confidence: 99%

Interaction of Arylsulfatase A with UDP-N-Acetylglucosamine:Lysosomal Enzyme-N-Acetylglucosamine-1-phosphotransferase

Schierau

Dietz

Lange

et al. 1999

Journal of Biological Chemistry

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The critical step in lysosomal targeting of soluble lysosomal enzymes is the recognition by an UDP-N-acetylglucosamine:lysosomal enzyme-N-acetylglucosamine-1-phosphotransferase. The structure of the determinant common to all lysosomal enzymes for proper recognition by the phosphotransferase is not completely understood. Our current knowledge is largely based on the introduction of targeted amino acid substitutions into lysosomal enzymes and analysis of their effects on phosphotransferase recognition. We have investigated the effect of eight anti-arylsulfatase A monoclonal antibodies on the interaction of arylsulfatase A with the lysosomal enzyme phosphotransferase in vitro. We also show that a lysine-rich surface area of arylsulfatases A and B is essential for proper recognition by the phosphotransferase. Monoclonal antibodies bind to at least six different epitopes at different locations on the surface of arylsulfatase A. All antibodies bind outside the lysine-rich recognition area, but nevertheless Fab fragments of these antibodies prevent interaction of arylsulfatase A with the phosphotransferase. Our data support a model in which binding of arylsulfatase A to the phosphotransferase is not restricted to a limited surface area but involves the simultaneous recognition of large parts of arylsulfatase A.

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“…Female BALB/c mice 6 weeks of age were injected three times intraperitoneally with 25 g of the partially purified TS forms adsorbed to 2 mg of Al(OH) 3 (Imject Alum, Pierce, Rockford, IL). Three days after the last injection spleen cells of one mouse was fused with non-secretor Ag8.653 myeloma cells (32) by the conventional polyethylene glycol-mediated fusion technique (33). After fusion, cells were plated in 288 wells of 24-well hybridoma plates (Greiner, Nü rtingen, Germany) in RPMI 1640 supplemented with 10% FCS, 100 units/ml penicillin, 100 g/ml streptomycin, 100 M hypoxanthine, 0.4 M aminopterin, and 16 M thymidine.…”

Section: Methodsmentioning

confidence: 99%

Two Trans-sialidase Forms with Different Sialic Acid Transfer and Sialidase Activities from Trypanosoma congolense

Tiralongo

Schrader²,

Lange

et al. 2003

Journal of Biological Chemistry

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Trypanosomes express an enzyme called trans-sialidase (TS), which enables the parasites to transfer sialic acids from the environment onto trypanosomal surface molecules. Here we describe the purification and characterization of two TS forms from the African trypanosome Trypanosoma congolense. The purification of the two TS forms using a combination of anion exchange chromatography, isoelectric focusing, gel filtration, and subsequently, antibody affinity chromatography resulted, in both cases, in the isolation of a 90-kDa monomer on SDS-PAGE, which was identified as trans-sialidase using micro-sequencing. Monoclonal antibody 7/23, which bound and partially inhibited TS activity, was found in both cases to bind to a 90-kDa protein. Both TS forms possessed sialidase and transfer activity, but markedly differed in their activity ratios. The TS form with a high transfer-to-sialidase activity ratio, referred to as TS-form 1, possessed a pI of pH 4 -5 and a molecular mass of 350 -600 kDa. In contrast, the form with a low transfer-to-sialidase activity ratio, referred to as TSform 2, exhibited a pI of pH 5-6.5 and a molecular mass of 130 -180 kDa. Both TS forms were not significantly inhibited by known sialidase inhibitors and revealed no significant differences in donor and acceptor substrate specificities; however, TS-form 1 utilized various acceptor substrates with a higher catalytic efficiency. Interestingly, glutamic acid-alanine-rich protein, the surface glycoprotein, was co-purified with TS-form 1 suggesting an association between both proteins.

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Appendix

Cited by 13 publications

References 0 publications

Thermal and non-thermal dust sputtering in hydrodynamical simulations of the multiphase interstellar medium

Thermal and non-thermal dust sputtering in hydrodynamical simulations of the multiphase interstellar medium

Interaction of Arylsulfatase A with UDP-N-Acetylglucosamine:Lysosomal Enzyme-N-Acetylglucosamine-1-phosphotransferase

Two Trans-sialidase Forms with Different Sialic Acid Transfer and Sialidase Activities from Trypanosoma congolense

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