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  • Polymer and Materials Science  (1)
  • mouse  (1)
  • 1
    ISSN: 0449-2951
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: Radiation-induced copolymerization of acrylonitrile with styrene was carried out over a wide range of temperatures. It was found that the rate of copolymerization is proportional to the square root of the dose rate. An apparent activation energy of 6.90 kcal./mole was obtained for the copolymerization in an equimolar mixture of monomers. The rate of copolymerization increased with the molar concentration of acrylonitrile in the monomer mixture. Monomer reactivity ratios were determined as rAN = 0.03, rSt = 0.33 for the copolymerization at 15 and 0°C., rAN = 0.28, rSt = 0 at -20°C. in the liquid state of monomers. On the other hand, the monomer reactivity ratios were obtained as rAN ≃ 0 and rSt ≃ 0 for the copolymerization in the solid state at -78°C. It was concluded from these experimental results that there is a great difference between the liquid-state and solid-state copolymerizations, both in the polymerization mechanism and the structure of copolymers.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 0730-2312
    Keywords: mouse ; PDI family proteins ; retinoic acid ; dibutyryl cAMP ; differentiation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: We investigated the expression of protein disulfide isomerase family proteins (PDI, ERp61, and ERp72) in mouse F9 teratocarcinoma cells during differentiation induced by treatment with retinoic acid and dibutyryl cAMP. Each member of this family was expressed at a constitutive level in undifferentiated F9 cells. During differentiation of F9 cells to parietal or visceral endodermal cells the protein level of all these enzymes increased, although the extent of this increase in both protein and mRNA levels varied among the enzymes. Certain proteins were found to be co-immunoprecipitated with PDI, ERp61, and ERp72 in the presence of a chemical crosslinker. Type IV collagen was significantly coprecipitated with PDI whereas laminin was equally coprecipitated with the three proteins. Furthermore, 210 kDa protein characteristically coprecipitated with ERp72. Thus, the induction of PDI family proteins during the differentiation of F9 cells and their association with different proteins may implicate specific functions of each member of this family despite the common redox activity capable of catalyzing the disulfide bond formation. J. Cell. Biochem. 68:436-445, 1998. © 1998 Wiley-Liss, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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