scholarly journals Toward a nanopaper-based and solid phase immunoassay using FRET for the rapid detection of bacteria

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Bentolhoda Heli ◽  
Abdellah Ajji
Keyword(s):  
Rapid Detection ◽  
Solid Phase ◽  
Solid Phase Immunoassay

A solid phase immunoassay for the rapid detection of Vibrio anguillarum in infected rainbow trout

Aquaculture ◽  
1987 ◽  
Vol 67 (1-2) ◽  
pp. 206
Author(s):  
E. Jansson ◽  
B. Sundqvist ◽  
E. Rivera ◽  
A. Thuvander ◽  
O. Ljungberg
Keyword(s):  
Rainbow Trout ◽  
Rapid Detection ◽  
Solid Phase ◽  
Vibrio Anguillarum ◽  
Solid Phase Immunoassay

Identification of hepatitis a virus in cell cultures by solid phase immune electron microscopy

1986 ◽  
Vol 44 ◽  
pp. 238-239
Author(s):  
C.D. Humphrey ◽  
T.L. Cromeans ◽  
E.H. Cook ◽  
D.W. Bradley
Keyword(s):  
Electron Microscopy ◽  
Liquid Phase ◽  
Cell Cultures ◽  
Rapid Detection ◽  
Hepatitis A ◽  
Hepatitis A Virus ◽  
Solid Phase ◽  
Immune Electron Microscopy ◽  
Detection And Identification

There is a variety of methods available for the rapid detection and identification of viruses by electron microscopy as described in several reviews. The predominant techniques are classified as direct electron microscopy (DEM), immune electron microscopy (IEM), liquid phase immune electron microscopy (LPIEM) and solid phase immune electron microscopy (SPIEM). Each technique has inherent strengths and weaknesses. However, in recent years, the most progress for identifying viruses has been realized by the utilization of SPIEM.

Performance Evaluation of the Phosphorescent Porphyrin Label:  Solid-Phase Immunoassay of α-Fetoprotein

2002 ◽  
Vol 74 (22) ◽  
pp. 5845-5850 ◽  
Author(s):  
Tomás C. O'Riordan ◽  
Aleksi E. Soini ◽  
Dmitri B. Papkovsky
Keyword(s):  
Performance Evaluation ◽  
Solid Phase ◽  
Solid Phase Immunoassay

A solid-phase immunoassay of protease-resistant prion protein with filtration blotting involving sodium dodecyl sulfate

2006 ◽  
Vol 349 (2) ◽  
pp. 218-228 ◽  
Author(s):  
Yoshiteru Kobayashi ◽  
Naoyuki Kohno ◽  
Shoko Wanibe ◽  
Kazunari Hirayasu ◽  
Hitoshi Uemori ◽  
...  
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Prion Protein ◽  
Solid Phase ◽  
Sodium Dodecyl ◽  
Solid Phase Immunoassay ◽  
Dodecyl Sulfate

Quantification of Lupus Anticoagulants in Clinical Samples Using Anti- β2GP1 and Anti-Prothrombin Monoclonal Antibodies

2001 ◽  
Vol 86 (08) ◽  
pp. 584-589 ◽  
Author(s):  
A. Le Querrec ◽  
J. Arnout ◽  
D. Arnoux ◽  
J. Y. Borg ◽  
C. Caron ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Lupus Anticoagulant ◽  
Solid Phase ◽  
Clinical Samples ◽  
Lupus Anticoagulants ◽  
Asymptomatic Patients ◽  
Solid Phase Immunoassay ◽  
Dependent Activity ◽  
Variable Contribution ◽  
Suitable Standard

SummaryQuantification of lupus anticoagulant (LA) in clinical samples is hampered by the lack of a suitable standard of activity. We evaluated the use of mAbs displaying LA activity for this purpose. As most patient samples contain both β2Glycoprotein I (β2GP1) and prothrombin dependent LA, a combination of two mAbs, one of each specificity, was added to normal plasma in a concentration from 0 to 60 g/ml. Eight assay systems using different reagents and instruments were used. The calibration curves were linear for all but one, with marked differences between the responsiveness to each mAb. A panel of plasmas from 69 patients with persistent LA diagnosed using the SSCISTH criteria was tested. An antiphospholipid syndrome (APS) was present in 40, whereas 29 were asymptomatic. LA activities of individual plasmas varied between assays (p <10–4), but homogeneous subgroups were identified. In a majority of samples, LA activity displayed a prothrombin-dependent profile, with a variable contribution of β2GP1-dependent activity. The latter was associated to β2GP1 antibodies detected by solid-phase immunoassay. By using 3 dilute Russell viper venom time assays, higher LA titers were found in APS, compared to asymptomatic patients (p <0.05).

scholarly journals IMMUNOLOGICAL IMBALANCE IN BREAST CANCER AND LUNG CANCER IN POSTMENOPAUSAL WOMEN

2018 ◽  
Vol 20 (6) ◽  
pp. 927-934 ◽  
Author(s):  
A. N. Glushkov ◽  
E. G. Polenok ◽  
L. A. Gordeeva ◽  
S. A. Mun ◽  
M. V. Kostyanko ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Lung Cancer ◽  
Postmenopausal Women ◽  
Marked Effect ◽  
Solid Phase ◽  
Anticancer Effect ◽  
Class A ◽  
Solid Phase Immunoassay ◽  
The One

Previous studies reported some associations between class A antibodies specific for benzo[a]pyrene (IgA-Bp), estradiol (IgA-Es) and progesterone (IgA-Pg) and breast cancer (BC) in women like as with lung cancer (LC) in men. It was suggested that IgA-Bp and IgA-Es may stimulate tumor initiation and promotion, whereas IgA-Pg may inhibit the in vivo human carcinogenesis.The purpose of this study was to identify the suggested associations of such immunological imbalance with BC and LC in postmenopausal women.The serum A-class antibodies specific to benzo[a]pyrene, estradiol and progesterone (IgA-Bp, IgA-Es, IgA- Pg) were studied in 335 healthy women, 824 breast cancer (BC) patients and 127 cases of lung cancer (LC) by means of non-competitive solid phase immunoassay. The following results were obtained: Increased ratio of IgA-Bp and IgA-Es amounts exceeding the IgA-Pg levels was associated with a higher risk of breast cancer (OR = 2.8 and 2.4 respectively, p < 0.0001), and higher risk of LC (OR = 2.9 and 2.8, respectively, p < 0.0001). Conversely, the OR values decreased to 0.3-0.4 for BC and LC if IgA-Pg levels were higher than IgA-Bp and IgA-Es levels (p < 0.0001). These findings confirm the hypothesis that IgA-Bp and IgA-Es are capable to stimulate, and IgA-Pg, to inhibit the BC and LC occurrence n postmenopausal women. The balance between IgA-Bp and IgA-Es, on the one hand, and IgA-Pg, on the other hand, is much more important than individual contents of these antibodies.In conclusion, the phenomenon of “immunological interference” is revealed, i.e., the mutual enhancement of IgA-Bp and IgA-Es effects, thus, probably, stimulating the initial and subsequent events of carcinogenesis initiation and promotion, with a weak anticancer effect of IgA-Pg, and by weakening the mutual procarcinogenic effects of IgA-Bp and IgA-Es by the marked effect of IgA-Pg.

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