Characterization of Recombinant Human Neuron-Specific Enolase and Its Application to Enzyme Immunoassay

Tumor Biology ◽  
1993 ◽  
Vol 14 (5) ◽  
pp. 261-270 ◽  
Author(s):  
Takashi Aoki ◽  
Masaya Kimura ◽  
Mitsuhiro Kaneta ◽  
Hiroe Kazama ◽  
Junji Morikawa ◽  
...  
1988 ◽  
Vol 34 (10) ◽  
pp. 2053-2057 ◽  
Author(s):  
S Raam ◽  
D M Vrabel

Abstract We present evidence to show that monoclonal antibodies to estrogen receptors (ER) in solid phase recognize the secondary estrogen binding sites with moderate to low affinity for estradiol (E2). An excellent quantitative agreement was found in five cytosols between the ER values obtained by the enzyme immunoassay (ER-EIA) and the amount of secondary estrogen binding sites measured by the assay involving dextran-coated charcoal (Clin Chem 1986;32:1496). The immunoreactive protein recognized by the antibody-coated beads, when allowed to react with ER(+) cytosols, is shown to bind [3H]estradiol only when the ligand concentration exceeds 8 nmol/L. Further biochemical and functional characterization of the immunoreactive protein is required to establish similarities/dissimilarities between this protein, high-affinity Type I ER sites, and the secondary sites such as Type II sites.


1991 ◽  
Vol 106 (1) ◽  
pp. 189-198 ◽  
Author(s):  
J. Fernández ◽  
A. M. Sandino ◽  
J. Pizarro ◽  
L. F. Avendaño ◽  
J. M. Pizarro ◽  
...  

SUMMARYHuman rotavirus isolates from 1100 stool samples were analyzed by polyacrylamide gel electrophoresis, and 48 different migration patterns were detected. Heterogeneity in the migration of segment 10 was observed in both long and short electropherotypes in which three long and two short patterns were identified. In spite of these variations all short and long electropherotypes were subgrouped by enzyme immunoassay as subgroups I and II respectively. Mixed infections were detected in 17% of cases and the subgrouping correlated with the corresponding electropherotypes. The same electropherotypes were present in severe, mild and asymptomatic cases and no electropherotype was particularly associated with greater virulence. Furthermore, the electropherotypes isolated from nosocomial asymptomatic cases were the same as those detected from those admitted with severe diarrheoa. It seems unlikely that electropherotyping can be used to identify more virulent strains of rotavirus.


2012 ◽  
Vol 26 (2) ◽  
pp. 304-314 ◽  
Author(s):  
Thallita Kelly Rabelo ◽  
Fares Zeidán-Chuliá ◽  
Laura Milán Vasques ◽  
João Paulo Almeida dos Santos ◽  
Ricardo Fagundes da Rocha ◽  
...  

2009 ◽  
Vol 92 (2) ◽  
pp. 487-495 ◽  
Author(s):  
Sujatha Nayak ◽  
Penmatsa Tanuja ◽  
Rao Beedu Sashidhar

Abstract A simple and sensitive indirect noncompetitive enzyme immunoassay to quantitate mercapturic acid-aflatoxin B1 (AFB1) adduct in rat urine is reported. A novel procedure was developed for in vitro synthesis of an immunogen, bovine serum albumen-glutathione-aflatoxin B1 (BSA-GSH-AFB1) using 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide hydrochloride. Sulphydryl group's analysis confirmed the conjugation of SH groups to AFB1. Thin-layer chromatography and spectral analysis (absorption, fluorescence, and Fourier transform infrared) of the conjugates further confirmed the formation of the adducts. Polyclonal antibodies specific to mercapturic acid-AFB1 adduct were produced against BSA-GSH-AFB1. The assay was found to be linear in the range of 100 pg100 ng of the analyte (y ab x). A 50 displacement of BSA-GSH-AFB1 antibodies was achieved at an inhibitory concentration (IC50)of 11.9 ng GSH-AFB1 (r2 0.98) and 1.22 ng N-acetyl-L-cysteine (NAC)-AFB1 (r2 0.98). Spiking 5 g/mL of reference standard to the control rat urine showed a recovery of 98 2. The immunoassay was validated in a rodent model exposed to a single oral dose of 1 mg/kg body mass of pure AFB1. The excretion of NAC-AFB1 adduct was quantitated at the end of 24 h. The concentration of the NAC-AFB1 adduct excreted in urine as determined by the immunoassay was found to be in the range of 3.225.97 g/mg creatinine. The present method may find wide application as a biochemical tool in molecular epidemiological and intervention studies with respect to human exposure to dietary aflatoxins.


Sign in / Sign up

Export Citation Format

Share Document