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  • 1
    Electronic Resource
    Electronic Resource
    Acute and protracted effects of intratracheal surfactant application on internal carotid blood flow velocity, blood pressure and carbondioxide tension in very low birth weight infants (1989)
    Springer
    European journal of pediatrics 148 (1989), S. 770-773 
    Details
    ISSN: 1432-1076
    Keywords: Surfactant treatment ; Preterm infants ; Dopplerultrasound ; Blood flow velocity ; Internal carotid artery
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract As a part of a multicentre clinical trial of prophylattic treatment with bovine surfactant (SF-RI 1) given to immature infants below 31 gestational weeks, short term and protracted effects on cerebral haemodynamics were assessed by Dopplersonographic measurements of the right internal carotid artery. Measurements were performed every 10 min for 1h after intratracheal application of the surfactant in ten treated infants. The results of additional measurements every 12h up to the age of 100h were compared with a control group. In single cases there were changes of time averaged mean maximum velocity (Vmax) of as much as 100% immediately after intratracheal surfactant application, although the mean short term and protracted variability of Vmax was the same as the protracted variability in the control group. Variability of mean arterial blood pressure and transcutaneous carbondioxide tension (tcpCO2) was even less. With proper adjustment of ventilatory settings intratracheal treatment with surfactant does not affect variability or absolute values of internal carotid Vmax, mean arterial blood pressure and transcutaneous pCO2 in low birth weight infants within 100h after application.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00443108
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  • 2
    Electronic Resource
    Electronic Resource
    Kinetic characterization of early intermediates in the folding of E. coli tryptophan-synthase β2 subunit (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 247-255 
    Details
    ISSN: 0887-3585
    Keywords: protein folding ; domain interactions ; fluorescence transfer ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: This report describes the use of fluorescence energy transfer between an intrinsic energy donor (tryptophan 177) and two chemically added acceptors to study intermediates in the folding of the β2 subunit of E. coli tryptophan-synthase. Two early folding steps are thus identified and characterized. One is very rapid (its rate constant at 12°C is 0.02 sec-1) and corresponds to the folding of the N-terminal domain into a structure whose overall features approximate well those of the native domain. The second step is somewhat slower (its rate constant at 12°C is 0.008 sec-1) and involves a conformational rearrangement of the N-terminal domain brought about by the interactions between the N-and C-terminal domains within a monomeric β chain. This brings to five the number of intermediates which have been identified and ordered on the folding pathway of the dimeric β2 subunit.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340010307
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Alternate succession of steps can lead to the folding of a multidomain oligomeric protein (1989)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 6 (1989), S. 395-404 
    Details
    ISSN: 0887-3585
    Keywords: folding pathway ; tryptophan synthase ; acid denaturation ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The β2 subunit of Escherichia coli tryptophan synthase can be either unfolded in 6 M guanidine, or extensively denatured at acidic pH. These two denatured form of β2 have different circular dichroism spectra and thus correspond to distinct physical states. Here we compare the folding pathways of these two different denatured forms of β chains. We describe the kinetics of regain of a variety of physical, functional, ad immunochemical signals characteristic of six successive steps previously identified on the folding pathway of guanidine unfolded β2. It is shown that whereas identical molecular events over with the same kinetics, the two folding pathways are different, and involve different structural intermediates.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340060406
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    Paper (German National Licenses)
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