Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.7.11.8 (FAST)
 758 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

This reports covers the application to paediatrics of total IgE determination by the means of a new direct, sandwich type, fluorescence enzyme immuno-assay (Fluoro-allergo sorbent test:FAST IgE). The technical process is adapted for usual determinations, in case of infants and young children, of low normal rates with a good sensitivity, and of high pathological rates. IgE total usual values are established by the FAST IgE test from serums of healthy children, aged from one day to 14 years. Seven age groups are to be distinguished.
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PMID:[Total serum IgE: normal pediatric values using the FAST IgE fluoroimmunoenzymatic technic]. 333 Nov 7

Orthorhombic crystals of the complex formed between bovine alpha-chymotrypsin and a recombinant human mucous proteinase inhibitor (SLPI) were grown. Data to 2.3 A resolution were collected on the area-detector diffractometer FAST. The crystal structure of the complex was solved by Patterson search techniques using chymotrypsin as a search model. A cyclic procedure of modeling and crystallographic refinement enabled the determination of the SLPI structure. The current crystallographic R-value is 0.19. SLPI has a boomerang-like shape with both wings comprising two well separated domains of similar architecture. In each domain the polypeptide chain is arranged like a stretched spiral. Two internal strands form a regular beta-hairpin loop which is accompanied by two external strands linked by the proteinase binding segment. The polypeptide segment of each domain is interconnected by four disulfide bridges with a connectivity pattern hitherto unobserved. The reactive site loop of the second domain has elastase and chymotrypsin binding properties. It contains the scissile peptide bond between Leu72I and Met73I and has a similar conformation to that observed in other serine proteinase protein inhibitors. Eight residues of this loop, two of the adjacent hairpin loop, the C-terminal segment and Trp30I are in direct contact with the cognate enzyme. The binding loop of the first domain (probably with anti-trypsin activity) is disordered due to proteolytic cleavage occurring in the course of crystallization.
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PMID:The 2.5 A X-ray crystal structure of the acid-stable proteinase inhibitor from human mucous secretions analysed in its complex with bovine alpha-chymotrypsin. 336 16

The purpose of this study is to assess the frequency of clinical sensitivity to Eastern White Pine Pollen, 100 consecutive patients with the seasonal (SAR) or perennial (PAR) allergic rhinitis seen in the allergy clinic were prick tested with pine pollen extract, 8-tree mixture, histamine and negative control. Positive skin test (ST) was defined as a wheal greater than 3 mm larger than control, plus flare. Patients with a positive ST were then asked to stop antihistamine and other related drug, for 48 hours and challenged in a double blind manner with increasing concentrations of intranasal pine extract, starting at 1/100,000 w/v, followed by 1/10,000, 1/1000 and 1/100 at 20 minute intervals. The dose given was 0.15 cc by metered dose spray; one nostril received pine extract diluted in saline, the other received plain saline,. Rhinometric measurements were obtained before and 20 minutes after each challenge. Positive challenges were defined as 1) subjective feeling of increased stuffiness or rhinorrhea and 2) greater than 25% decrease in nasal airflow. Six patients (6%) had a positive ST to pine pollen extract and two of four patients with positive pine skin test had a positive FAST. Four of these were challenged intranasally, 2 had a positive challenge. All six patients had a history of spring SAR and positive reaction to 8-tree mix. Out of the 100 patients skin tested, 61 had spring SAR; therefore, the incidence of positive ST to pine in patients with spring SAR was 6/61 (10%). We conclude that pine pollen can be a cause of spring SAR in the New England area.
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PMID:Eastern pine sensitivity in New England. 341 92

The IgG4 is the predominant antibody response in patients receiving chronic exposure to high doses of antigen, and this seems to be true for immunotherapy as well. The duration and the dose of immunotherapy (IT) seems to increase specific IgG4 levels, but this increase does not seem to be related to the clinical response, seasonal exposure, duration of disease, and IgE antibody levels. The measurement of IgE and IgG4 antibodies to allergens did not predict the clinical effect of immunotherapy in our study. However, it indicated that the patients were continuing to receive the allergenic extracts and that the extract used in vivo, although produced by a different manufacturer, was closely resembling the one used for coating plastic wells in the FAST assay. The increase of antibody titres demonstrate that long term monitoring of IT administration may be accomplished by these in vitro tests, although individual patients may exhibit different responses in time but similar clinical results. Longitudinal studies on a cohort of atopic subjects may help define more precisely doses and timings required to achieve useful indications on both compliance with IT injections and predictivity of its outcome.
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PMID:IgE and IgG4 levels in allergic patients during immunotherapy. 348 27

A solid phase Sepharose-based RIA (IgG4 RAST) was compared to the IgG4 FAST enzyme immunoassay for measurements of Ragweed-specific IgG4. Although FAST reagents were used, a standard serum of known antibody content along with modifications in the FAST assay were necessary to attempt to develop a quantitative assay. Various assay parameters such as precision, reproducibility, sensitivity and parallelism were examined. Specificity of the monoclonal anti-IgG4 used in the FAST was not evaluated. Conditions and method of assay for the two systems differed substantially, particularly in the short incubation times for the IgG4 determinations.
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PMID:A comparison study between ragweed-specific IgG4 as measured by RAST and FAST. 348 28

The bilin binding protein of the butterfly Pieris brassicae has been prepared, crystallized and its crystal structure determined at high resolution using film and FAST area detector intensity data. The crystallographic asymmetric unit contains a tetramer of identical subunits with a molecular weight of about 90,000. The crystal structure was determined by isomorphous replacement. Use was made of the molecular symmetry to improve phases. A molecular interpretation of the electron density distribution and partial tracing of the polypeptide chain was possible without amino acid sequence information, as the fold is very similar to retinol binding protein. It is characterized by a beta-barrel formed by two orthogonal beta-sheets and an alpha-helix. The bilin pigment seems to be bound within the beta-barrel analogously to retinol in retinol binding protein. The tetramer in the crystal has C2 symmetry and is a dimer of dimers of quasi-equivalent subunits.
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PMID:Crystallization, crystal structure analysis and preliminary molecular model of the bilin binding protein from the insect Pieris brassicae. 365 19

Starting from a population of genetically heterogeneous mice, selective breeding is being used to develop lines differing in sensitivity to ethanol-induced open-field activity. Mice are tested twice for 4 min in an open field. The first test is between min 2-6 after injection of saline. Twenty-four hr later, a similar test is performed after injection of ethanol (1.5 g/kg). Two independent FAST lines are being selected for ethanol-induced increases in activity, and two independent SLOW lines are being selected for ethanol-induced decreases. After four generations of selection, the lines have diverged significantly. These lines should be useful for exploring the neuropharmacological basis for the activating and rewarding properties of ethanol.
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PMID:Mice genetically selected for differences in open-field activity after ethanol. 365 83

The FAST assay (Allergenetics) for the determination of specific IgE has recently been introduced. The results of this test, graded in classes 0 (negative), 1 (equivocal) and 2 to 6 (positive) were compared with those of another commercially available test (Phadezym RAST, Pharmacia), graded from class 0 (negative) and classes 1 to 4 (positive). In 52 adults suffering from rhinitis/asthma, a total of 114 positive skin prick tests (SPT) were obtained for common respiratory allergens. In 67% of these tests the Phadezym RAST was positive and in 63% the FAST was positive (classes 2 to 6). In these patients there were 151 negative SPT: 6% corresponded to a positive Phadezym RAST (all class 1) and 34% to a positive FAST (classes 2 to 6). The serum of nine nonatopic volunteers who had negative SPT for 12 common allergens were tested. In none did the Phadezym RAST give any positive results; the FAST was positive in all nine sera, detecting between five and 11 allergens. When both assays were performed on 14 unselected cord blood samples, the Phadezym RAST was positive in three samples (with class 1 results to a maximum of two allergens), and the FAST was positive in 12 samples, detecting between one and seven allergens. Thus, in our hands, the FAST gave an abnormally high number of positive results in patients with negative SPT, in nonatopic volunteers, and in cord blood.
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PMID:Comparison of two assays for the determination of specific IgE in serum of atopic and nonatopic subjects: the Allergenetics FAST and the Phadezym RAST. 375 16

The Falcon assay screening test (F.A.S.T.) system was used to develop a rapid, sensitive, and quantitative kinetic-based enzyme-linked immunosorbent assay (k-ELISA) for detecting antibodies against Schistosoma mansoni adult microsomal antigens (MAMAs). The FAST-ELISA uses polystyrene beads on sticks molded to the lid of a microtitration plate. The beads are coated with antigen. Reagents and sera are placed in microtitration plates and the beads exposed to reagents by immersion. The exposure time required for a single dilution of serum or other antibody source, conjugate, and substrate is 5 min each. Excluding preparation time, two plates can easily be assayed in 30 min. The optima for assay conditions, reproducibility, quantitative linearity, and sensitivity are delineated. A battery of sera from patients with both homologous and heterologous infections was tested, and a dilution series of a standard reference serum pool was included with each test. Results were expressed in number of units as calibrated against the standard reference sera pool. Antigen-coated bead storage studies were performed with untreated and three chemically treated antigens. The storage stability of MAMA, ability to perform the assay with minimal equipment, sensitivity, short assay time, and ease of operation make the FAST-ELISA ideal for field studies.
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PMID:Development and optimization of the FAST-ELISA for detecting antibodies to Schistosoma mansoni. 376 May 81

With the described method it is possible to determinate residues of Dapsone (DDS) and its acetylated metabolites (mono- and diacetyldapsone) in milk. The determination is being carried out with a FAST-LC system (Fully Automated Sample Treatment Liquid Chromatography). The purification is a combination of dialysing the milk against water and absorption of the nonpolar components from the dialysate on the preconcentration column of the LC-system used (RP, 40 microns). With back-flush, the concentrate is being injected into the analytical column (RP-8, 5 microns). The detection is being carried out with the help of a UV-absorbance detector, at a wavelength of 296 mm. The detection limit is approximately 2 micrograms/l (DADDS: 5 micrograms/l). The required amount of the sample is 5 ml. The recovery, reproducibility and linearity for the three components in milk are good.
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PMID:[Automated determination of 4,4'-diaminodiphenylsulfone (DDS) and acetyl metabolites (MADDS and DADDS) in milk with the FAST-LC system]. 376 55


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