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  • Biochemistry and Biotechnology  (2)
  • Fuchs heterochromic cyclitis  (2)
  • 1
    Digitale Medien
    Digitale Medien
    Springer
    International ophthalmology 19 (1995), S. 169-171 
    ISSN: 1573-2630
    Schlagwort(e): Fuchs heterochromic cyclitis ; uveitis ; Amsler sign ; aqueous humor ; hyphema
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract To investigate the frequency and diagnostic significance of Amsler's sign in patients with Fuchs' heterochromic cyclitis (FHC), we performed a diagnostic AC puncture of the eyes of 31 patients with this disease and looked for the same sign in 104 patients with intermediate uveitis and 373 patients with various other types of uveitis who underwent the same procedure. AS was significantly more frequent in the FHC patients than in either of the other two groups of patients, and occurred infrequently in all other types of chronic uveitis. We therefore consider its occurrence to have important differential diagnostic value. We would also emphasize the pathophysiologic significance of AS and suggest that this aspect should be investigated in the future.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    ISSN: 1573-2630
    Schlagwort(e): aqueous humor ; Fuchs heterochromic cyclitis ; IgG subclass ; herpetic uveitis ; toxoplasmic chorioretinitis
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract Changes in local immunity are important whenconsidering the physiopathology of uveitis. The aim ofthis study was to measure IgG and IgG subclassconcentrations in the serum and the AH of patients withthree different types of uveitis and to determine for eachof them the presence of a local production of IgG in theintra-ocular compartment. This investigation was extendedto IgG subclasses.Serum and AH of 46 patients, including 11 with Fuchsheterochromic cyclitis (FHC), 13 with toxoplasmicchorioretinitis, 11 with herpetic uveitis and 11 with senilecataract (taken as controls) were analyzed by ELISA forIgG and IgG subclasses. Three quotients (r1, IgG/albuminin serum; r2, IgG/albumin in AH; and R, r2/r1) werecalculated in order to estimate the local synthesis (LS) ofIgG and each IgG subclass.In AH of patients with herpetic uveitis, a concomitant andsignificant increase of all IgG subclasses as well asalbumin (with no significant increase of r2 or R) wasobserved. This finding was interpreted as an indirectconsequence of major damage to the blood–aqueousbarrier. In patients with FHC, a significant increase of r2and R involving only the IgG1 subclass was observed,indicating the existence of LS of IgG1 in the majority ofthese patients. In the AH of patients with toxoplasmicchorioretinitis, no significant modification of IgG subclassor albumin concentrations was observed when comparedto controls.In conclusion, it would seem interesting to considermeasurement of IgG and IgG subclasses and calculationof the coefficients r1, r2 and R for a better evaluation ofthe local immunological processes observed in differenttypes of uveitis.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 3
    Digitale Medien
    Digitale Medien
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 247-255 
    ISSN: 0887-3585
    Schlagwort(e): protein folding ; domain interactions ; fluorescence transfer ; Chemistry ; Biochemistry and Biotechnology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Medizin
    Notizen: 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.
    Zusätzliches Material: 5 Ill.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 4
    Digitale Medien
    Digitale Medien
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 6 (1989), S. 395-404 
    ISSN: 0887-3585
    Schlagwort(e): folding pathway ; tryptophan synthase ; acid denaturation ; Chemistry ; Biochemistry and Biotechnology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Medizin
    Notizen: 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.
    Zusätzliches Material: 3 Ill.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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