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  • Polymer and Materials Science  (1)
  • preoperative examination  (1)
  • 1
    ISSN: 1573-0743
    Keywords: aortic aneurym ; transesophageal echocardiography ; thrombus ; prognosis ; preoperative examination
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Transesophageal echocardiography (TEE) was performed in 17 cases of aortic aneurysms referred to our hospital for further examination and treatment. All 17 cases were treated surgically and TEE was performed as a preoperative examination. In nine of the 17 cases, there were already some signs of bleeding upon admission and in all of these nine cases, rupture of the aneurysm was confirmed during surgery. Measurement on cross-sectional TEE imaging disclosed large aneurysmal diameters in eight of these nine cases, suggesting a close relationship between diameter and rupture. Moreover, observation of the lesions by TEE suggested a relationship between the risk of rupture and morphological characteristics of the thrombus. In seven of the nine bleeding cases, TEE imaging revealed destructive features of the aneurysmal thrombus, such as exfoliation from the aortic wall and/or tearing-off, suggesting expansion of the aortic diameter. Detailed findings of the aneurysm and thrombus on TEE corresponded with surgical findings. Thus, we concluded that TEE is a useful method of obtaining information about aortic aneury sms not only as a preoperative examination but also as an independent examination to determine treatment options and prognosis.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Biopolymers 38 (1996), S. 733-744 
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Oxidative folding of ο-conotoxin MVIIC, a highly basic 26-amino acid peptide with three disulfide bonds, predominantly gave two products with mismatched disulfide bonds in 0.1M NH4OAc buffer (pH 7.7) at 21°C both in the presence and absence of redox reagents such as reduced and oxidized glutathione. A low reaction temperature (5°C) and a high salt concentration in buffer such as 2M (NH4)2SO4 were necessary to obtain the correctly folded biologically active product. The folding reaction was found to proceed via a two-stage pathway of (I) the formation and (II) the rearrangement of the mismatched disulfide bonds. Both the reaction temperature and the salt strongly affected the equilibrium between mismatched and correctly formed disulfide bonds in the second stage. Such an effect of salts on the rearrangement reaction could be explained by anion binding at a low concentration and the salting out effect at a high concentration by analyzing the rank order of their effectiveness. The anion-binding effect was also confirmed by examining the folding of the tetra-acetylated peptide at the Lys side chains. CD study suggested that the yield of the biologically active product was correlated with its conformational change as functions of temperature and salt concentration. © 1996 John Wiley & Sons, Inc.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
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