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New polypeptide components purified from mamba venom
Author(s) -
Tytgat Jan,
Vandenberghe Isabel,
Ulens Chris,
Van Beeumen Jozef
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02201-3
Subject(s) - venom , trypsin , biochemistry , chemistry , amino acid , chromatography , enzyme , biology
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 IC 50 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.