期刊论文详细信息
FEBS Letters
New polypeptide components purified from mamba venom
Van Beeumen, Jozef1  Vandenberghe, Isabel1  Tytgat, Jan2  Ulens, Chris2 
[1] Laboratory of Protein Biochemistry and Protein Engineering, University of Gent, Ledeganckstraat 35, B-9000 Gent, Belgium;Laboratory of Toxicology, University of Leuven, E. Van Evenstraat 4, B-3000 Leuven, Belgium
关键词: Snake;    Mamba;    Venom;    Toxin;    Polypeptide;    Potassium;   
DOI  :  10.1016/S0014-5793(01)02201-3
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 摘 要 】

New polypeptide components have been isolated from Dendroaspis angusticeps venom using chromatography. Two polypeptides containing 59 and 57 amino acids, called ‘DaE1’ and ‘DaE2’ respectively, have been purified to homogeneity and fully sequenced. Spectrometric analysis yielded masses of 6631.5 and 6389.0 Da, respectively. The polypeptides share 98 and 95% identity, respectively, with trypsin inhibitor E (DpE) of Dendroaspis polylepis polylepis. ‘DaE’ polypeptides inhibit Kv1.1 channels with an IC50 value in the range of 300 nM. They can be considered as new dendrotoxins, albeit with fairly low affinity as compared to α-DTX. ‘DaE’ polypeptides do not affect Kir2.1 channels.

【 授权许可】

Unknown   

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