Production and characterization of anti-nisin Z monoclonal antibodies: suitability for distinguishing active from inactive forms through a competitive enzyme immunoassay

2001 ◽  
Vol 56 (1-2) ◽  
pp. 114-119 ◽  
Author(s):  
L. Daoudi ◽  
C. Turcotte ◽  
C. Lacroix ◽  
I. Fliss
Keyword(s):  
Monoclonal Antibodies ◽  
Enzyme Immunoassay ◽  
Nisin Z

scholarly journals Characterization of Chemotactic Responses and Flagella of Hyphomicrobium Strain W1-1B

1998 ◽  
Vol 180 (11) ◽  
pp. 3003-3006 ◽  
Author(s):  
Laura Tuhela ◽  
Jayne B. Robinson ◽  
Olli H. Tuovinen
Keyword(s):  
Monoclonal Antibodies ◽  
Enzyme Immunoassay ◽  
Electron Micrographs ◽  
Smooth Surface ◽  
Rhizobium Meliloti ◽  
Surface Pattern ◽  
Polyacrylamide Gels ◽  
Western Blots

ABSTRACT Motile swarmer cells of Hyphomicrobium strain W1-1B displayed positive chemotactic responses toward methylamine, dimethylamine, and trimethylamine but did not display significant chemotactic responses towards methanol and arginine. Electron micrographs of negatively stained intact flagellar filaments indicated a novel striated surface pattern. The flagella were composed of two proteins of 39 and 41 kDa. Neither protein was a glycoprotein as determined by Schiff’s staining and by enzyme immunoassay. Protein fingerprints visualized from silver-stained polyacrylamide gels and Western blots of protease-digested samples indicated that the two proteins were similar but not identical. Monoclonal antibodies prepared to the complex flagella of Rhizobium meliloti cross-reacted with the striated flagella of Hyphomicrobium strain W1-1B; however, these antibodies did not cross-react with smooth-surface flagella. These results suggest that complex and striated flagella possess homologous epitope regions.

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.

scholarly journals Arachidonate 5-lipoxygenase of porcine leukocytes studied by enzyme immunoassay using monoclonal antibodies.

1987 ◽  
Vol 262 (14) ◽  
pp. 6741-6745
Author(s):  
S Kaneko ◽  
N Ueda ◽  
T Tonai ◽  
T Maruyama ◽  
T Yoshimoto ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Enzyme Immunoassay
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