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Cold spin

Hence, if the crystal is initially in a magnetically ordered state at (lattice) temperature T (hot lattice + cold spins), but is then demagnetized under adiabatic conditions (q = 0), the entropy of spin disordering must be drawn from the crystal lattice (because no heat can exchange with the surroundings), and the lattice temperature drops ... [Pg.184]

Figure 13.7 Examples of heat-integrated columns that can experience startup problems, (o) A typical cryogenic gas plant demethanizer that can experience cold spins (b) a heat-integrated column that can experience surging. Figure 13.7 Examples of heat-integrated columns that can experience startup problems, (o) A typical cryogenic gas plant demethanizer that can experience cold spins (b) a heat-integrated column that can experience surging.
An example of the first type is the use of low-acid, low-salt, and low-temperature spin-baths, which slow down the cellulose regeneration sufficiently to yield HWM polynosic rayon [190]. Another example is the Lilienfeld process for which the viscose, made from unaged alkali cellulose with excess carbon disulfide and only a short ripening, is spun into a cold spin-bath containing 50-85% of sulfuric acid. This is a case of stabilizing the xanthic acid. Rayon produced in this way has tenacities greater than 5 g/den. [Pg.729]

Figure 9.6. CuCb-stained gel of SDS PAGE shows purification of (GVGVP)25i by phase separation. (Lane 1) Lyse-transformed cell showing all E. coli proteins plus the bulging band of product, (GVGVP)25i. (Lane 2) Residue of the cold spin where the protein-based polymer plus most E. coli protein remained in solution. (Lane 3) Supernatant of 37°C warm spin that contains essentially all of the remaining E. coli protein. (Lane 4) Model protein, (GVGVP)2si, phase separated at 37°C from the E. coli protein that remained in solution (lane 3). (Reproduced with permission from Urry et al. )... Figure 9.6. CuCb-stained gel of SDS PAGE shows purification of (GVGVP)25i by phase separation. (Lane 1) Lyse-transformed cell showing all E. coli proteins plus the bulging band of product, (GVGVP)25i. (Lane 2) Residue of the cold spin where the protein-based polymer plus most E. coli protein remained in solution. (Lane 3) Supernatant of 37°C warm spin that contains essentially all of the remaining E. coli protein. (Lane 4) Model protein, (GVGVP)2si, phase separated at 37°C from the E. coli protein that remained in solution (lane 3). (Reproduced with permission from Urry et al. )...
Leo P, Tiesinga E, Julienne PS, Walter DK, Kadlecek S, Walter TG. (1998) Elastic and inelastic collisions of cold spin-polarized Cs atoms. Phys. Rev. Lett. 81 1389-1392. [Pg.549]

Discard the supernatant, resuspend the cells pellet in 4 ml of ice-cold lysis buffer, and spin cells again as in step 2. [Pg.202]

Transfer the culture into an ice-cold 50-ml tube and immediately spin down the cells at 4000 rpm for 4 min at 4°. [Pg.223]

Spin at 9500 rpm ( 8200y) for 5 min at 4° and transfer the supernatant into a new cold microfuge tube. This step removes most of the cell debris, leaving a cleared lysate. [Pg.224]


See other pages where Cold spin is mentioned: [Pg.184]    [Pg.184]    [Pg.300]    [Pg.301]    [Pg.184]    [Pg.184]    [Pg.300]    [Pg.301]    [Pg.300]    [Pg.301]    [Pg.368]    [Pg.369]    [Pg.483]    [Pg.493]    [Pg.527]    [Pg.4]    [Pg.184]    [Pg.184]    [Pg.300]    [Pg.301]    [Pg.184]    [Pg.184]    [Pg.300]    [Pg.301]    [Pg.300]    [Pg.301]    [Pg.368]    [Pg.369]    [Pg.483]    [Pg.493]    [Pg.527]    [Pg.4]    [Pg.205]    [Pg.134]    [Pg.265]    [Pg.317]    [Pg.347]    [Pg.421]    [Pg.65]    [Pg.232]    [Pg.233]    [Pg.147]    [Pg.383]    [Pg.418]    [Pg.252]    [Pg.439]    [Pg.57]    [Pg.1005]    [Pg.428]    [Pg.174]    [Pg.925]    [Pg.141]    [Pg.28]    [Pg.35]    [Pg.23]    [Pg.202]    [Pg.202]   
See also in sourсe #XX -- [ Pg.368 ]




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