Research on the C-terminal domain of ADAMTS13 regulates its cleaving activity / 中华血液学杂志
Chinese Journal of Hematology
;
(12): 830-834, 2010.
Article
Dans Chinois
| WPRIM
| ID: wpr-353543
ABSTRACT
<p><b>OBJECTIVE</b>To study the influence of C-terminal domain of ADAMTS13 on its cleaving activity.</p><p><b>METHODS</b>The full-length wild-type (WT) and C-terminal domain truncated type (TT, TSP8 + CUB domains were deleted) of human ADAMTS13 recombinant protein were transfected into and permanent expressed on Hela cells. Western blot and R-CBA were used to directly detect the activities of the two recombinant proteins under the static and stressed condition respectively. ELISA was used to compare the binding abilities of the two proteins by coating with vWF.</p><p><b>RESULTS</b>The recombinant proteins were identified by Western blot with anti-his-tag or anti-ADAMTS13 antibodies. With pretreatment of 1.5 M urea, the enzyme activity of TT was significantly higher than that of WT, and so did in binding ability with vWF While, only WT could cleave vWF under high stress.</p><p><b>CONCLUSION</b>The distal carboxyl-terminal TSP8 together with CUB domains of ADAMTS13 may affect the enzyme activity by regulating the binding of ADAMTS13 to vWF in different conditions, and they are very important for the enzyme activity under high stress force condition.</p>
Texte intégral:
Disponible
Indice:
WPRIM (Pacifique occidental)
Sujet Principal:
Protéines recombinantes
/
Facteur de von Willebrand
/
Transfection
/
Galium
/
Génétique
/
Métabolisme
Type d'étude:
Étude pronostique
Limites du sujet:
Humains
langue:
Chinois
Texte intégral:
Chinese Journal of Hematology
Année:
2010
Type:
Article
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