Library

feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
  • Coeliac disease  (3)
  • Polymer and Materials Science  (3)
  • AML1 gene  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Hematology and cell therapy 38 (1997), S. 183-186 
    ISSN: 1279-8509
    Keywords: Secondary leukemia ; translocation ; t(16;21) ; AML1 gene
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract A t(16;21)(q24;q22) translocation was detected by fluorescence in situ hybridization in a patient with acute myeloblastic leukemia previously treated for malignant lymphoma. While the breakpoint on chromosome 21 was within the AML1 gene as determined by FISH, the gene partner on chromosome 16 could not be identified. Band 16q24 appears to be rearranged in several types of myeloid proliferation and a review of the literature shows that these rearrangements most often occur in secondary leukemia and myelodysplastic syndrome or are part of complex chromosomal rearrangements.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 2
    ISSN: 1432-1076
    Keywords: Diagnostic value ; Gliadin IgG, IgA, and IgE antibody determinations ; Coeliac disease
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The diagnostic value of gliadin IgG, IgA and IgE antibody (AB) determinations using the fluorescent immunosorbent test was examined in 586 children with malabsorptive disorders and/or failure to thrive. All patients underwent jejunal biopsy and were on a gluten-containing diet. IgG AB were found in all patients (331/331) with untreated coeliac disease (CD) in our study, but IgA AB in only 295/331 (89%). Therefore a screening test based only on IgA AB determinations is not recommended. By contrast, 203 (80%) of 255 children with other malabsorptive disorders had no gliadin AB, 43 (16.5%) had only IgG AB and only 9 (3.5%) had IgG and IgA AB. IgE AB proved to be of no additional value as a diagnostic tool because they were found in a quarter of the children without CD. Statistical evaluation of combined IgG and IgA AB determination showed at least 96% sensitivity and a specificity of 97%. The subjective (“Bayesian”) probability that an actual patient with a given AB test result has CD, is considered: a patient very probably has CD in the case of positive IgG and IgA AB, and no CD in the case of a negative AB result. In the case of negative IgA AB but positive IgG AB the physician's judgement (“prior probability”) influences the (“posterior”) probability of CD for an actual patient. In contrast to IgG AB, IgA AB decline rapidly after the introduction of a gluten-free diet and may be used for diet control after diagnosis. Antibodies against cow's milk proteins, though present in 72% of the 331 patients with CD, are of no therapeutic significance in CD and are of no value for its diagnosis.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 3
    ISSN: 1432-1076
    Keywords: Diagnosis ; Cow's milk protein intolerance ; Fluorescent immunosorbent test ; IgG-, IgE-, IgA-, IgM-antibodies to casein ; β-lactoglobulin ; α-lactalbumin ; Bovine serum albumin and gliadin ; Gastro-enteritis ; Coeliac disease
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Antibodies of various immunoglobulin classes to different cow's milk proteins were studied with the fluorescent immunosorbent test in 601 newborns, infants, children and adults (A). The antibody levels, expressed as the geometric mean (gm) of four antibody titres to casein, β-lactoglobulin, α-lactalbumin and bovine serum albumin, showed a clear dependence on age. They were compared with the antibody levels in children with cow's milk protein intolerance (C), other gastrointestinal disorders (B) and coeliac disease (D). The 20 children with cow's milk protein intolerance clearly differed (significance level 2×10-11) from those of the two control groups (A, B) insofar as the criterion adopted was not the titre against a single protein but the gm of the four antibody titres, and insofar as allowance was made for the age of the patients. All patients with cow's milk protein intolerance also showed elevated gm titres of IgE, IgA and IgM antibodies. However, since a number of children in the control groups also showed higher values, particularly with regard to IgE antibodies, the determination of the IgE, IgA and IgM antibodies adds little to the diagnosis and at best provides a further discriminatory aid. Although antibody titres fall immediately after placing the child on a milk-free diet, it is a matter of months before they become negative (titre 〈1∶20). After challenge titres rise again. In a longitudinal study of 25 children with acute gastroenteritis (E) it was shown that the antibody titres remained unchanged during and after the attack. This contradicts the often expressed opinion that the cow's milk antibodies frequently observed in healthy infants are induced as a consequence of gastroenteritis. In contrast to the other groups, all 26 children with proven coeliac disease (D) had antibodies to gliadin, irrespective of whether their gm cow's milk antibody titre was high or low.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 4
    ISSN: 1432-1076
    Keywords: Coeliac disease ; Different dietary conditions ; Fluorescent immunosorbent test for IgG gliadin antibodies ; Leucocyte migration inhibition test with gluten subfractions B2 and B3
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The diagnostic value of the fluorescent immunosorbent test for IgG gliadin antibodies (FIST) has been investigated in comparison with the LIF test—the competence of the gluten subfractions B2 and B3 in releasing lymphokines from peripheral lymphocytes in vitro—in 96 patients with coeliac disease (CD) under various dietary conditions. In untreated children with CD during their first 2 years of life, the FIST showed 100% sensitivity with 95% specificity, whilst the LIF test showed only 70% sensitivity and 73% specificity. Therefore it can be concluded that the FIST as a screening test is superior to the LIF. In older children with a proved recurrence of the mucosal abnormality after reintroduction of a normal diet, only 44% showed increased IgG gliadin antibody titres whereas 70% proved to be positive in the LIF test. Under a controlled gluten challenge all six patients reacted with a distinct increase in gliadin antibody titres whereas the LIF test changed from positive to negative and vice versa without following any clear principle. These results emphasize the inadequacy of the LIF test as a diagnostic method, both in untreated CD and under controlled gluten challenge.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 5
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Biopolymers 19 (1980), S. 899-911 
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The heats of ionization of protons, ΔHi, of oxidized and reduced horse heart cytochrome c in 0.15M KCl at 20°C were determined using a titration calorimeter which simultaneously afforded the potentiometric titration curve. Reproducibility of the thermal titrations is within 2%, and evaluation of the heats observed after the heat loss corrections is estimated to be within 5%. A single titration of oxidized cytochrome c from pH 11 to 3 is in excellent agreement with the thermal titration of this protein obtained with flow calorimetry. The thermal titration, however, is not reversible, due in part to the loss of titratable group(s) in this pH region and to the heat contribution of the acid and alkaline conformational changes which occur. Although of lesser magnitude, the reduced form also indicates similar thermal transitions. These differences are due solely to conformational contributions to the thermal process, since the potentiometric curves are reversible. The nature of the irreversibility for oxidized cytochrome c appears to involve the loss of a group with pK′ 8.9 and the shift of two groups from pK′ 5.6 to 4.8. Thermal difference curves for this process indicate that heats of -7.8 and -24.1 kcal/mol are liberated which are centered at pH 9.3 and 3.9, respectively.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 6
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Simultaneous curve fitting for the ionization parameters of oxidized and reduced horse heart cytochrome c in 0.15M KCl and 20°C yields values for the ionization constants (as pK′) and the heats of ionization (ΔHi) which can reconstruct either the potentiometric or thermal titration curves. Reduced cytochrome c requires 8 sets of groups, whereas oxidized cytochrome c requires 10 sets of groups. The additional groups in the oxidized preparation appear to involve the ferriheme (pK′, 9.25; ΔHi, 13.7 kcal/mol) and a tyrosine (pK′ ≃ 10.24) that is not present in the reduced form. The potentiometric and thermal difference curves (reduced - oxidized) involve the appearance of 17 kcal/mol centered at pH 9.7 and 5.8 kcal/mol centered at pH 4.9. The carboxyl groups in both species appear to be normal for the hydrogen-bonded form. Only one histidine has normal ionization properties (pK′, 6.7; ΔHi, 7.5 kcal/mol), as do 17 of the lysine residues (pK′, 10.8; ΔHi, 11.5 kcal/mol).
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 7
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Biopolymers 19 (1980), S. 885-898 
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Potentiometric titration curves of oxidized and reduced horse heart cytochrome c in 0.15M KCl at 20°C have been obtained by timed titration (0.125-0.500 μmol/sec) from the isoionic points (pH 10.2-10.4) to pH 3 and back to the isoionic point. Computer-assisted (PROPHET) data acquisition and blank corrections give curves with good precision with a maximum standard deviation of 0.3 groups for an average error of 1%. The potentiometric titration curve of reduced cytochrome c is reversible within the precision of the method and for the pH range studied. The potentiometric curves for oxidized cytochrome c titrated upscale (pH 3-10) and downscale (pH 10-3) are not reversible. However, they show the same ionization behavior after the initial downscale titration. This is probably the result of a conformational change. Comparison of the data herein reported with the titration curves of oxidized cytochrome c already published by others indicates good agreement on the basis of a normalization of the concentration of protein or on the basis of 25 titrable groups between the acid end point and the isoionic pH.Titration of the 2 μmol imidazole in the upscale or downscale direction gives the correct analytical concentration and pK′ after correction for the solvent titration. Titration of reduced cytochrome c in the presence and absence of an additional equivalent of imidazole gave a difference titration curve, which indicates that a group on the protein shifts from pK′ 5.8 to pK′ 5.3 in the presence of imidazole. The pK′ of imidazole, in the presence of the protein, remains at a nearly normal value of 7.34.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...