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Isolation and characterization of hi...

Richard, Gabrielle.

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Isolation and characterization of high affinity VHH antibody fragments against alpha-cobratoxin.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Isolation and characterization of high affinity VHH antibody fragments against alpha-cobratoxin./
Author:	Richard, Gabrielle.
Description:	117 p.
Notes:	Source: Masters Abstracts International, Volume: 48-05, page: 2946.
Contained By:	Masters Abstracts International48-05.
Subject:	Biology, Molecular. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=MR58412
ISBN:	9780494584125

Isolation and characterization of high affinity VHH antibody fragments against alpha-cobratoxin.
Richard, Gabrielle.

Isolation and characterization of high affinity VHH antibody fragments against alpha-cobratoxin. - 117 p.

Source: Masters Abstracts International, Volume: 48-05, page: 2946.

Thesis (M.Sc.)--University of Guelph (Canada), 2010.

Camelid VHHs may provide better treatment for snake envenomation than conventional antivenom antibodies because of their smaller size (&sim;16 kDa), better tissue permeability and lower immunogenicity. In this thesis, a phage-displayed VHH library with 4.2 x 109 functional clones was constructed from a Ilama hyperimmunized with crude Thai cobra ( Naja kaouthia) venom. After three rounds of panning against acobratoxin (alpha-Cbtx), a potent neurotoxin from the Thai cobra venom, 26 unique clones were found using monoclonal phage ELISA and confirmed by DNA sequencing. Surface plasmon resonance (SPR) analyses showed that the four selected anti-alpha-Cbtx VHH clones had dissociation constants (KD) in the low nanomolar range (0.4-25 nM)and that these four VHHs bound to the same or overlapping epitopes on alpha-Cbtx. An in vitro muscle twitch assay showed that VHH C2 (KD = 0.4nM) effectively neutralized the paralytic effects of alpha-Cbtx at neuromuscular junctions.

ISBN: 9780494584125Subjects--Topical Terms:

1017719
Biology, Molecular.

Isolation and characterization of high affinity VHH antibody fragments against alpha-cobratoxin.
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100 1 $a Richard, Gabrielle. $3 1682883
245 1 0 $a Isolation and characterization of high affinity VHH antibody fragments against alpha-cobratoxin.
300 $a 117 p.
500 $a Source: Masters Abstracts International, Volume: 48-05, page: 2946.
502 $a Thesis (M.Sc.)--University of Guelph (Canada), 2010.
520 $a Camelid VHHs may provide better treatment for snake envenomation than conventional antivenom antibodies because of their smaller size (&sim;16 kDa), better tissue permeability and lower immunogenicity. In this thesis, a phage-displayed VHH library with 4.2 x 109 functional clones was constructed from a Ilama hyperimmunized with crude Thai cobra ( Naja kaouthia) venom. After three rounds of panning against acobratoxin (alpha-Cbtx), a potent neurotoxin from the Thai cobra venom, 26 unique clones were found using monoclonal phage ELISA and confirmed by DNA sequencing. Surface plasmon resonance (SPR) analyses showed that the four selected anti-alpha-Cbtx VHH clones had dissociation constants (KD) in the low nanomolar range (0.4-25 nM)and that these four VHHs bound to the same or overlapping epitopes on alpha-Cbtx. An in vitro muscle twitch assay showed that VHH C2 (KD = 0.4nM) effectively neutralized the paralytic effects of alpha-Cbtx at neuromuscular junctions.
590 $a School code: 0081.
650 4 $a Biology, Molecular. $3 1017719
650 4 $a Biology, Microbiology. $3 1017734
650 4 $a Health Sciences, Immunology. $3 1017716
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