Serological characterization of potato isolates ofErwinia carotovorasubsp.atrosepticaand subsp.carotovorausing polyclonal and monoclonal antibodies

1995 ◽  
Vol 79 (6) ◽  
pp. 592-602 ◽  
Author(s):  
B. Alarcón ◽  
M.T. Gorris ◽  
M. Cambra ◽  
M.M. López
Keyword(s):  
Monoclonal Antibodies ◽  
Serological Characterization

Serological Characterization of Hungarian Plum Pox Virus Isolates

1997 ◽  
Vol 52 (5-6) ◽  
pp. 391-395
Author(s):  
Juan José López-Moya ◽  
Dionisio López-Abella ◽  
José-Ramón Díaz-Rúiz ◽  
Belén Martinez-Garcia ◽  
Richard Gáborjányi
Keyword(s):  
Monoclonal Antibodies ◽  
Coat Protein ◽  
Blot Analysis ◽  
Plum Pox Virus ◽  
Rt Pcr ◽  
Dot Blot ◽  
Serological Characterization ◽  
Spanish Isolate ◽  
Virus Isolates

Abstract Three Hungarian (No.2, 4 and 9), and a Moldavian (K) plum pox virus isolates were compared with a characterized Spanish isolate (5.15) by RT-PCR, ELISA, dot-blot and West­ern blot analysis. Monoclonal antibodies prepared against the external, intermediate and internal sequences of the coat protein of the Spanish isolate were able to differentiate the four isolates. Hungarian isolate No. 2 proved to be serologically identical to the Spanish isolate, while No. 4 showed appreciable differences and No. 9 could be recognized only by the monoclonal antibodies representing the intermedial and internal parts of the coat protein. K isolate showed a more distant relationship to other isolates. Our experiment provided the first demonstration of the presence of D type isolates in Hungary.

Serological Characterization of Murine Monoclonal Antibodies Directed against Acquired B Red Cells

Vox Sanguinis ◽  
1990 ◽  
Vol 59 (2) ◽  
pp. 92-95
Author(s):  
D. Janvier ◽  
S. Veaux ◽  
M. Reviron ◽  
F. Guignier ◽  
M. Benbunan
Keyword(s):  
Monoclonal Antibodies ◽  
Red Cells ◽  
Serological Characterization ◽  
Murine Monoclonal Antibodies

Production of monoclonal antibodies to prune dwarf ilarvirus and their use in the serological characterization of almond virus isolates

EPPO Bulletin ◽  
1997 ◽  
Vol 27 (4) ◽  
pp. 555-556 ◽  
Author(s):  
A. BOARI ◽  
D. BOSCIA ◽  
M. YURTMEN ◽  
O. POTERE ◽  
C. TORTURO ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Serological Characterization ◽  
Virus Isolates

Serological Characterization of Murine Monoclonal Antibodies Directed against Acquired B Red Cells

Vox Sanguinis ◽  
1990 ◽  
Vol 59 (2) ◽  
pp. 92-95 ◽  
Author(s):  
D. Janvier ◽  
S. Veaux ◽  
M. Reviron ◽  
F. Guignier ◽  
M. Benbunan
Keyword(s):  
Monoclonal Antibodies ◽  
Red Cells ◽  
Serological Characterization ◽  
Murine Monoclonal Antibodies

scholarly journals Generation and Serological Characterization of Murine Monoclonal Antibodies against O Antigens from Acinetobacter Reference Strains

2001 ◽  
Vol 8 (4) ◽  
pp. 825-827 ◽  
Author(s):  
Ralph Pantophlet ◽  
Lore Brade ◽  
Helmut Brade
Keyword(s):  
Monoclonal Antibodies ◽  
Enzyme Immunoassay ◽  
High Specificity ◽  
Culture Collections ◽  
O Antigen ◽  
Serological Characterization ◽  
O Antigens ◽  
Reference Strains ◽  
Murine Monoclonal Antibodies

ABSTRACT O-antigen-specific monoclonal antibodies were generated againstAcinetobacter strains from international type culture collections and characterized by enzyme immunoassay and Western and colony blotting. The antibodies aid in the further completion of an O-serotyping scheme for Acinetobacter and, due to their high specificity, are especially useful to all working with these strains.

Characterization of Monoclonal Anti-human Factor VII Antibody (B101/B1) that Recognized Three-dimensional Structures near Arg at Position 79 in the First EGF-like Domain

1998 ◽  
Vol 79 (01) ◽  
pp. 104-109 ◽  
Author(s):  
Osamu Takamiya
Keyword(s):  
Monoclonal Antibodies ◽  
Tissue Factor ◽  
Human Factor ◽  
Solid Phase ◽  
Three Dimensional ◽  
Coagulation Factors ◽  
Factor Vii ◽  
Dimensional Structure ◽  
Epidermal Growth

SummaryMurine monoclonal antibodies (designated hVII-B101/B1, hVIIDC2/D4 and hVII-DC6/3D8) directed against human factor VII (FVII) were prepared and characterized, with more extensive characterization of hVII-B101/B1 that did not bind reduced FVIIa. The immunoglobulin of the three monoclonal antibodies consisted of IgG1. These antibodies did not inhibit procoagulant activities of other vitamin K-dependent coagulation factors except FVII and did not cross-react with proteins in the immunoblotting test. hVII-DC2/D4 recognized the light chain after reduction of FVIIa with 2-mercaptoethanol, and hVIIDC6/3D8 the heavy chain. hVII-B101/B1 bound FVII without Ca2+, and possessed stronger affinity for FVII in the presence of Ca2+. The Kd for hVII-B101/B1 to FVII was 1.75 x 10–10 M in the presence of 5 mM CaCl2. The antibody inhibited the binding of FVII to tissue factor in the presence of Ca2+. hVII-B101/B1 also inhibited the activation of FX by the complex of FVIIa and tissue factor in the presence of Ca2+. Furthermore, immunoblotting revealed that hVII-B101/B1 reacted with non-reduced γ-carboxyglutaminic acid (Gla)-domainless-FVII and/or FVIIa. hVII-B101/B1 showed a similar pattern to that of non-reduced proteolytic fragments of FVII by trypsin with hVII-DC2/D4 on immunoblotting test. hVII-B101/B1 reacted differently with the FVII from the dysfunctional FVII variant, FVII Shinjo, which has a substitution of Gln for Arg at residue 79 in the first epidermal growth factor (1st EGF)-like domain (Takamiya O, et al. Haemosta 25, 89-97,1995) compared with normal FVII, when used as a solid phase-antibody for ELISA by the sandwich method. hVII-B101/B1 did not react with a series of short peptide sequences near position 79 in the first EGF-like domain on the solid-phase support for epitope scanning. These results suggested that the specific epitope of the antibody, hVII-B101/B1, was located in the three-dimensional structure near position 79 in the first EGF-like domain of human FVII.

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