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  • 1995-1999  (2)
  • 1960-1964
  • Reactivities of chymotrypsin  (1)
  • Tobacco BY-2 cells  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Effects of gelation of alginate around chymotrypsin on reactivities (1997)
    Springer
    Colloid & polymer science 106 (1997), S. 257-261 
    Details
    ISSN: 1435-1536
    Keywords: Reactivities of chymotrypsin ; gelation of alginate ; immobilized enzyme ; effects of gelation ; capsule
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: Abstract To elucidate adding effects of alginate (Alg) and its gelation on the reactivities of chymotrypsin (Chy), three kinds of Chy-immobilized capsules were prepared by an interfacial condensation, i.e., (a) a capsule containing only Chy in the core (Chy capsule), (b) a capsule containing Chy in NaAlg (Chy capsule(NaAlg)) and (c) a capsule containing Chy in CaAlg gel (Chy capsule(CaAlg)). The coated film was poly(ethylenediamine-terephthaloyl) (PEDT) and NaAlg in the core was gelled in the state adhered tightly to the PEDT film. These Chyimmobilizing capsules were found to be useful for determining the effects of the gelation around Chy. 4-nitrophenyl acetate was used as a substrate. From the rates of efflux of the product (p-nitrophenol), apparent maximum velocitiesv max and the apparent Michaelis constantsK′m were obtained. The values ofv′max showed the maximum at pH=7.8 for all three capsules and were found not to show any pH shift. The magnitude ofv′max was in the following order: Chy capsule (CaAlg) 〉 Chy capsule (NaAlg)-Chy capsule. The adding effects of Alg and its gelation on the reactivities of Chy are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01189533
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Sites of microtubule reorganization in tobacco BY-2 cells during cell-cycle progression (1997)
    Springer
    Protoplasma 198 (1997), S. 202-209 
    Details
    ISSN: 1615-6102
    Keywords: Cell cycle ; Elongation factor 1α ; Microtubule reorganization ; Microfilament ; Tobacco BY-2 cells
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The sites of microtubule (MT) reorganization were examined in synchronized tobacco BY-2 cells. The MTs of these cells were completely destroyed by a combined cold and drug treatment at 0 °C with 100 μM propyzamide for 3 h. After the cells were washed and cultured at 30 °C, the reorganization of MTs was observed in detail. Sites for MT reorganization at each stage of the cell cycle were identified on the cell cortex and nuclei, the mitotic apparatus, the nuclei (or the nuclei and cell cortex), and the cell cortex in the S-G2 phase, M phase, M/G1 interface, and g1 phase, respectively. The polypeptide synthesis elongation factor (EF)-1α is co-localized with these sites of MT reorganization. At some stages, microfilaments (MFs) were found to be involved in the reorganization of MTs. Based on these results, the mode of MT reorganization during cell cycle progression is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01287569
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    Paper (German National Licenses)
    Fulltext
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