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  • Activation  (1)
  • Bovine serum albumin and gliadin  (1)
  • Gastro-enteritis  (1)
  • 1
    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
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  • 2
    ISSN: 1617-4623
    Keywords: Bacillus thuringiensis ; Crystal protein ; Activation ; Lepidoptera ; Toxic fragment
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The amino acid sequences necessary for entomocidal activity of the CryIA(b) protoxin of Bacillus thuringiensis were determined. Introduction of stop codons behind codons Arg601, Phe604 or Ala607 showed that amino acid residues C-terminal to Ala607 are not required for insecticidal activity and that activation by midgut proteases takes place distal to Ala607. The two shortest polypeptides, deleted for part of the highly conserved β-strand, were prone to proteolytic degradation, explaining their lack of toxicity. Apparently, this β-strand is essential for folding of the molecule into a stable conformation. Proteolytic activation at the N-terminus was investigated by removing the first 28 codons, resulting in a translation product extending from amino acid 29 to 607. This protein appeared to be toxic not only to susceptible insect larvae such as Manduca sexta and Heliothis virescens, but also to Escherichia coli cells. An additional mutant, encoding only amino acid residues 29–429, encompassing the complete putative pore forming domain, but lacking a large part of the receptor-binding domain, was similarly toxic to E. coli cells. This suggests a role for the N-terminal 28 amino acids in rendering the toxin inactive in Bacillus thuringiensis, and indicates that the cytolytic potential of the pore forming domain is only realized after proteolytic removal of these residues by proteases in the insect gut. In line with this hypothesis are results obtained with a mutant protein in which Arg28 at the cleavage site was replaced by Asp. This substitution prevented the protein from being cleaved by trypsin in vitro, and reduced its toxicity to M. sexta larvae.
    Type of Medium: Electronic Resource
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