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Song, K.J.,Ko, R.K.,Kim, H.S.,Ha, H.S.,Ha, D.W.,Oh, S.S.,Park, C.,Yoo, S.-I.,Kim, M.W.,Kim, C.J.,Joo, J.H. Institute of Electrical and Electronics Engineers 2007 IEEE transactions on applied superconductivity Vol.17 No.2
<P>The degree of ferromagnetism of Ni-W<SUB>y</SUB> alloys decreases as W-content y increases. Both the saturation magnetization <I>M</I> <SUB>sat</SUB> and Curie temperature <I>T</I> <SUB>c</SUB> decrease linearly with W-content y, and both <I>M</I> <SUB>sat</SUB> and <I>T</I> <SUB>c</SUB> go to zero at critical concentration of y<SUB>c</SUB> ~9.50 at.% W. To compare with Ni-W alloys, the magnetic properties of a series of both as-rolled (non-textured) and annealed (biaxially textured) [Ni<SUB>97at.%</SUB>-W<SUB>3at.%</SUB>]<SUB>100-x</SUB>-Cu<SUB>x</SUB> alloy tapes with compositions x = 0, 1, 3, 5, and 7 at.%, were studied. Characterization methods included XRD analyses to investigate the biaxial texturing of the annealed [Ni-W]-Cu alloy tapes and studies of the magnetization for both as-rolled and annealed [Ni-W]-Cu alloy tapes. Both the isothermal mass magnetizations <I>M</I>(<I>H</I>) of a series of samples at different fixed temperatures and <I>M</I>(<I>T</I>) in fixed field, were measured. The effect of Cu addition on both the saturation magnetization and Curie temperature T<SUB>c</SUB> of the Ni<SUB>97at.%</SUB>-W<SUB>3at.%</SUB> alloy was investigated.</P>
Park, E-Y,Kim, W-Y,Kim, Y-M,Lee, J-H,Han, K-H,Weiner, I D,Kim, J Gutenberg 2012 HISTOLOGY AND HISTOPATHOLOGY Vol.27 No.12
<P>Potassium depletion (K?-D) induces hypertrophy and hyperplasia of collecting duct cells, and potassium repletion (K?-R) induces regression of these changes. The purpose of this study was to examine the time courses of the changes in cellular composition, the origin of intercalated cells (ICs) and the mechanism responsible for these changes. SD rats received K?-depleted diets for 1, 7, or 14 days. After K?-D for 14 days some of the rats received normal diets for 1, 3, 5, or 7 days. In the inner stripe of the outer medulla, K?-D increased significantly the number and proportion of H?-ATPase-positive ICs, but decreased the proportion of H?-ATPase-negative principal cells (PCs). However, proliferation was limited to H?-ATPase-negative PCs. During K?-R, the cellular composition was recovered to control level. Apoptosis increased during K?-R and exclusively limited in H?-ATPase-negative PCs. Double immunolabeling with antibodies to PC and IC markers identified both cells negative or positive for all markers during both K?-D and K?-R. Electron microscopic observation showed that ultrastructure of AE1-positive some cells were similar to AE1-negative some cells during K?-R. LC3 protein expression increased significantly and autophagic vacuoles appeared particularly in PCs on days 14 of K?-D and in ICs on days 3 of K?-R. These results suggest that PCs and ICs may interconvert in response to changes in dietary K+ availability and that autophagic pathways may be involved in the interconversion.</P>
Lee, H. G,P. Y. Lee,Y. K. Lee,S. J. Kim,H. K. Chung,M. K. Seo,J. K. Park,K. S. Min,W. K. Chang 한국동물생명공학회(구 한국동물번식학회) 2003 Reproductive & developmental biology Vol.27 No.4
The effects of additions/deletions in glycosylated residues of recombinant human EPO (rhEPO) produced in CHO-K1 on their secretion were examined. hEPO cDNA was amplified from human liver mRNA and cloned into the pCR2.1 TOPO. Using overlapping-extension site-directed mutagenesis method, glycosylation sites at 24th, 38th, 83rd, and 126th were respectively or accumulatively removed by substituting its asparagine (or serine) with glutamine. To add novel glycosylation sites, 69 and 105th leucine was mutated to asparagine. Mutant and wild type rhEPO constructs were cloned into the pcDNA3 expression vector with CMV promoter and transfected into CHO cell line, CHO-K1, to produce mutant rhEPO mutant rhEPO proteins. Enzyme-linked immunosorbant assay (ELISA) and Western analysis with monoclonal anti-EPO antibody were performed using supernatants of the cultures showing transient and stable expressions respectively. Addition of novel glycosylation reduced rhEPO secretion dramatically while deletion mutants had little effect except some double deletion mutants (△24/83 and △38/83) and triple mutant (△24/38/83). This fact suggests that not single but combination of changes in glycosyl groups affect secretion of rhEPO in cell culture, possibly via changes in their conformations.