Abstract：
:Two distinct families of low-molecular-weight toxins (argiotoxins) have been isolated from the venom of the orb-web spider. Argiope trifasciata. The toxins have been purified to homogeneity and characterised by spectroscopic, mass spectrometric and microchemical analysis. The major biologically active member of the first family of toxins is 2,4-dihydroxyphenylacetyl-asparagine linked through a C11-tetra-amine to N-terminal arginine; other members of this family are methylene homologues. The second family of toxins possesses an indolic group in place of the 2,4-dihydroxyphenyl chromophore. The toxins act as non-competitive inhibitors at quisqualate-type glutamatergic receptors on a metathoracic retractor unguis nerve-muscle preparation of Schistocerca gregaria. The loss of the N-terminal arginine reduces biological activity of the first family of toxins, but not of the second. The nature of the polyamine appears to be less important, perhaps acting as a spacer between the cationic arginine and the more hydrophobic aromatic tail of the toxins.
journal_name
Brain Resjournal_title
Brain researchauthors
Budd T,Clinton P,Dell A,Duce IR,Johnson SJ,Quicke DL,Taylor GW,Usherwood PN,Usoh Gdoi
10.1016/0006-8993(88)91098-0subject
Has Abstractpub_date
1988-05-10 00:00:00pages
30-9issue
1eissn
0006-8993issn
1872-6240pii
0006-8993(88)91098-0journal_volume
448pub_type
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