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)

In the steady-state free precession (SSFP) with an applied linear gradient, the transverse magnetizations are periodically distributed. Fourier analysis of this periodic distribution leads to the understanding of many interesting phenomena in SSFP. It is found that there are many other higher-order echoes in SSFP in addition to the previously known echoes. By deriving general description of the transverse magnetization of SSFP and by expanding the echo time independent term with Fourier series, the higher-order echoes including the two previously known FISP and CE-FAST are understood and explained. These higher-order echoes are studied in detail by both computer simulation and experiments and their results are reported.
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PMID:Analysis of the higher-order echoes in SSFP. 204 35

We report a new type of SSFP imaging sequences for acquiring higher-order echoes. Spins excited during a cycle have, in a sense, a phase memory such that they can be refocused several cycles down the line, and since the spins are pulsed under a steady-state condition, the resulting echoes have very complicated T1 and T2 dependencies. A steady-state equation, which describes the T1 and T2 dependencies for the higher-order echoes, is presented, and the intensity of each echo is calculated and compared with the experimental results. Although the signal intensity of the higher-order echoes are weaker than the FID or the CE-FAST echo, these echoes may be used to obtain images with different contrast dependencies previously unobtainable with either of the two signals.
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PMID:Multiple echo SSFP sequences. 206 37

Selectively bred FAST mice are highly susceptible, while SLOW mice are less susceptible, to the locomotor stimulant effects of ethanol. Heritability estimates indicate that approximately 15% of the variance in the FAST lines is of additive genetic origin, while low susceptibility is ostensibly nonheritable. Inbreeding has increased at the rate of 2% per generation, but fertility has been unaffected. Measurement reliability for sensitivity to this ethanol effect was high when measured in both circular (r = 0.6) and square (r = 0.7) open-fields. In addition, our results indicate that we have selected for differences in sensitivity to ethanol rather than for differences in habituation to the test environment. The difference in response to ethanol between FAST and SLOW mice extended to tests varying in duration, and to a range of ethanol doses. We conclude that the divergence between FAST and SLOW mice generalizes to related test parameters, and speculate that the genetic architecture underlying the locomotor stimulant response may be simpler than previously proposed.
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PMID:Response to selection for ethanol-induced locomotor activation: genetic analyses and selection response characterization. 206 90

A high-performance gel chromatography (HPGC) system has been developed which allows the unattended on-line determination of lipoprotein cholesterol distribution (VLDL-C, LDL-C, HDL-C), within 40 min, in microliter quantities of plasma using a single, relatively inexpensive column (Superose 6HR). The FAST cholesterol reagent (Sclavo) and a knitted PFTE Kratos reaction coil (Applied Biosystems) were found to provide optimal sensitivity, linearity, resolution, and dispersion characteristics. Validation is provided by comparison to target values for human quality control reference sera, and by comparing the values obtained by HPGC to the beta-quant method (LRC). The utility of the system is illustrated by comparing profiles from seven different species with normal or elevated plasma cholesterol concentrations. This technique allows rapid analysis of samples, regardless of species, without the use of precipitating agents or the ultracentrifuge. It could also be applied for the direct clinical determination of LDL-cholesterol.
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PMID:Rapid on-line determination of cholesterol distribution among plasma lipoproteins after high-performance gel filtration chromatography. 207 44

The study involved 117 adults and 535 children with atopic dermatitis. Immunoglobulins E against D. pteronyssinus--main allergen of the home dust--were assayed with RAST technique in children and FAST technique in adult patients. It was found that the blood serum IgE levels increase with patients' age and is the highest in patients with coexisting allergic respiratory diseases (difference statistically significant). RAST precision was compared with that of "prick" skin tests in the detection of allergy to home dust mites. Desensitization of 15 patients with home mite allergen produced satisfactory effects.
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PMID:[Sensitivity to the primary house dust allergen--dermatophagoides pteronyssinus--in patients with atopic dermatitis]. 209 37

The Falcon assay screening test-enzyme-linked immunosorbent assay (FAST-ELISA) and the enzyme-linked immunoelectrotransfer blot (EITB) technique were used to test human sera with Dracunculus medinensis adult worm antigen in order to assess their potential value in the immunodiagnosis of dracunculiasis. The human sera used were from patients with prepatent and patent D. medinensis infections or from patients infected with other nematodes (Onchocerca volvulus and Loa loa) or trematodes (Schistosoma mansoni and S. haematobium), as well as uninfected Nigerian and Puerto Rican normal controls. In the FAST-ELISA, the sera from prepatent and patent dracunculiasis patients gave the highest absorbance values relative to normal human sera. The highest cross-reactivity was observed with onchocerciasis sera; no cross-reactivity was seen with sera from individuals with loiasis or schistosomiasis mansoni or haematobia. By the EITB, sera from dracunculiasis patients specifically recognized a 16 kDa protein (Dm 16) and antibodies to Dm 16 disappeared 2 months after worm extraction. Recognition of Dm 16 occurred from the late prepatent stage. A 17 kDa protein (Dm 17) was also recognized by dracunculiasis sera, but antibodies to Dm 17 disappeared more slowly and were present 1 year after recovery. The 16 kDa and 17 kDa antigens of D. medinensis may be useful in the immunodiagnosis of dracunculiasis.
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PMID:Immunodiagnosis of dracunculiasis by Falcon assay screening test-enzyme-linked immunosorbent assay (FAST-ELISA) and by enzyme-linked immunoelectrotransfer blot (EITB) technique. 214 63

The accuracy of measurement using kits in the clinical laboratories is important for the patient diagnosis and treatment. In the present paper, the AL-18, AlaSTAT, CAP, FAST and RAST methods were investigated and were compared among kits the results obtained with serum sample, for determination of specific IgE antibodies. Significant differences among kits were observed from the results of those methods. One of the reasons, why the data discrepancy exists, is that each kit uses a different reference and a different inclusion method of allergen. For the evaluation of data discrepancy among those kits, it might be important that the clinical history of symptoms and in vivo tests against the different allergens compared with results of in vivo tests.
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PMID:[A comparison of the several methods for determination of specific IgE antibodies]. 224 59

The crystal and molecular structure of trypsin at a transiently stable intermediate step during catalysis has been determined by X-ray diffraction methods. Bovine trypsin cleaved the substrate p-nitrophenyl p-guanidinobenzoate during crystallization under conditions in which the acyl-enzyme intermediate, (guanidinobenzoyl)trypsin, was stable. Orthorhombic crystals formed in space group P2(1)2(1)2(1), with a = 63.74, b = 63.54, and c = 68.93 A. This is a crystal form of bovine trypsin for which a molecular structure has not been reported. Diffraction data were measured with a FAST (Enraf Nonius) diffractometer. The structure was refined to a crystallographic residual of R = 0.16 for data in the resolution range 7.0-2.0 A. The refined model of (guanidinobenzoyl)trypsin provides insight into the structural basis for its slow rate of deacylation, which in solution at 25 degrees C and pH 7.4 exhibits a t1/2 of 12 h. In addition to the rotation of the Ser-195 hydroxyl away from His-157, C beta of Ser-195 moves 0.7 A toward Asp-189 at the bottom of the active site, with respect to the native structure. This allows formation of energetically favorable H bonds and an ion pair between the carboxylate of Asp-189 and the guanidino group of the substrate. This movement is dictated by the rigidity of the aromatic ring in guanidinobenzoate--model-building indicates that this should not occur when arginine, with its more flexible aliphatic backbone, forms the ester bond with Ser-195. As a consequence, highly ordered water molecules in the active site are no longer close enough to the scissile ester bond to serve as potential nucleophiles for hydrolysis.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Structure of an acyl-enzyme intermediate during catalysis: (guanidinobenzoyl)trypsin. 225 95

Comparison of the three-dimensional structure of bovine chymosin with the structures of homologous aspartic proteinases complexed with peptide inhibitors shows that Val111 in chymosin occupies a position between the specificity subsites S1 and S3. A mutation corresponding to Val111 to Phe has been introduced in an intermediary plasmid construct of prochymosin by bridging its unique restriction sites by a synthetic mutant oligonucleotide duplex. A prochymosin fusion product was expressed in Escherichia coli in such a way that the extension and substitution of the propart does not interfere with the activation of the zymogen. After activation of the crude prochymosin, the enzyme was purified by affinity chromatography on Sepharose with V-dL-P-F-F-V-dL as ligand. This procedure provided large amounts of pure protein as judged by FPLC, the activity/protein ratio, and SDS-PAGE. The enzymatic properties were determined by using a variety of peptide substrates and inhibitors; KM values for the mutant enzyme were approximately twice those of the wild type, but the kcat values were little changed. The mutant enzyme was crystallized, X-ray data were collected to 2.0-A resolution by using a FAST area detector, and the structure was solved by using difference Fourier methods and refined to an R factor of 19.5%. The mutation leads to only local changes in conformation, with the phenylalanine side chain occupying part of the S1 and S3 pockets. This accounts for the increased KM of this mutant for a substrate with a large phenylalanine side chain at P1. It is also consistent with the higher affinity of the mutant for an inhibitor with small side chains at P1 and P3 when compared with the wild-type enzyme.
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PMID:Engineering enzyme subsite specificity: preparation, kinetic characterization, and X-ray analysis at 2.0-A resolution of Val111Phe site-mutated calf chymosin. 227 25

In 79 males aged 19-21 years with acute and chronic urticaria living under similar conditions the levels were determined of total IgE (FIST test) and specific IgE (FAST test) against the most frequent inhaled and food allergens. Statistically significant rise of the mean value of total IgE was noted in both groups of patients. In acute urticaria increased concentration of specific IgE against inhaled allergens was significantly more common.
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PMID:[IgE levels and hypersensitivity to certain inhaled and food allergens in acute and chronic urticaria]. 228 42


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