PubMed · 3633820
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A N Mal'tseva. 1986. [Allergy].. https://pubmed.ncbi.nlm.nih.gov/3633820/
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OBJECTIVE: To compare cutaneous reactivity to insect and arachnid allergens in clinically normal (control) and allergic dogs in the southeastern United States. DESIGN: Prospective, controlled study. ANIMALS: 26 clinically normal dogs and 82 allergic dogs from the southeastern United States. PROCEDURE: Intradermal skin testing with various dilutions of 13 insect and arachnid allergens was performed on control dogs to establish skin threshold concentrations (ie, concentrations to which < 25% of the dogs had positive reactions). These established threshold concentrations were then used to test allergic dogs for reactivity. Prevalence of single and multiple insect and arachnid reactions were determined. RESULTS: Flea allergen was the only allergen that caused a significantly higher prevalence of positive reactions in allergic dogs than in control dogs. CLINICAL IMPLICATIONS: Flea hypersensitivity is the most important arthropod hypersensitivity in dogs. The importance of reactivity to insect and arachnid allergens other than flea allergen can be determined only when prevalence of positive reactivity has been determined in an appropriate regional control group of dogs.
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The crystal structure of the cucumber basic protein (CBP), a type 1 or blue copper protein, has been refined at 1.8 A resolution. The molecule resembles other blue copper proteins in having a Greek key beta-barrel structure, except that the barrel is open on one side and is better described as a "beta-sandwich" or "beta-taco". The Cu atom has the normal blue copper NNSS' co-ordination with bond lengths Cu-N(His39) = 1.93 A, Cu-S(Cys79) = 2.16 A, Cu-N(His84) = 1.95 A, Cu-S(Met89) = 2.61 A. The Cu-S(Met) bond is the shortest so far observed in a blue copper protein. A disulphide link, (Cys52)-S-S-(Cys85), appears to play an important role in stabilising the molecular structure. It is suggested that the polypeptide fold is typical of a sub-family of blue copper proteins (phytocyanins) as well as a non-metalloprotein, ragweed allergen Ra3, with which CBP has a high degree of sequence identify. The proteins currently identifiable as phytocyanins are CBP, stellacyanin, mavicyanin, umecyanin, a cucumber peeling cupredoxin, a putative blue copper protein in pea pods, and a blue copper protein from Arabidopsis thaliana. In all except CBP and the pea-pod protein, the axial methionine ligand normally found at blue copper sites is replaced by glutamine. The structure of CBP was originally solved by the multiple wavelength anomalous scattering method, using data recorded at four wavelengths. All these data were included in the restrained least squares refinement. The final model comprises 96 amino acid residues, 122 solvent molecules and a copper atom. Several residues are modelled as having more than one conformation. The residual R is 0.141 for 41,910 observations (including Bijvoet-related observations) of 8.142 unique reflections in the resolution range 7 to 1.8 A.