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Purification, cloning and characterization of a metalloproteinase from

发布日期:2011.09.03 访问次数: 字号:[ ]


The complement systemis a very important part of the immune system.Many snake venoms
possess activities that influence the complement. A newmetalloproteinase (termed atrase B)
with anticomplementary activitywas purified fromNaja atra venom. Atrase B is a single chain
glycoproteinwith amolecularmass of 49.4 kDa and an isoelectric point of 9.7. Its N-terminal
sequence shows high homology to those ofmetalloproteinases fromcobra venoms. The cDNA
sequence reveals that atrase B is a PIII classmetalloproteinase. Atrase B slowly cleaves the A
chain of fibrinogen. It also exhibits edema-inducing activity, but has no hemorrhagic activity
and proteolytic activity against fibrin, azocasein, and N-benzoyl-L-arginine ethyl ester. Inter-
estingly, atrase B inhibits activation of the complement classical and alternative pathways in
a dose- and time-dependent manner. Complement components factor B and C6 are major
targets for atrase B to cleave. Atrase B is the first identified SVMP that cleaves complement
components factor B, C6, C7, and C8.
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