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- Brown, Mark A., et al.
(author)
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Detection of vitamin K-dependent proteins in venoms with a monoclonal antibody specific for gamma-carboxyglutamic acid.
- 2002
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In: Toxicon. - 0041-0101. ; 40:4, s. 447-453
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Journal article (peer-reviewed)abstract
- gamma-Carboxyglutamic acid (Gla) is an unusual amino acid that is synthesized post-translationally from glutamate in a vitamin K-dependent reaction. The dicarboxylic side chain of Gla chelates Ca(2+), a property important for the biological activity of vitamin K-dependent proteins. To date, Gla-containing polypeptides have been identified in venom from two groups of organisms: elapid snakes, and snails of the genus Conus. In certain elapid snakes, a gamma-carboxylated coagulation factor Xa-like protein is a component of the venom whereas cone snails utilize Gla in a range of peptide neurotoxins. Using a monoclonal antibody that specifically recognizes Gla residues, venom samples from various organisms were screened by western blotting and immunofluorescence assays. Amino acid analyses were also performed on most samples. A survey of 21 snake species from 12 genera detected gamma-carboxylated polypeptides only in venom of snakes from the elapid subfamily Acanthophiinae. Gla-containing polypeptides were also observed in cone snail venom but not in venom or toxic salivary secretions from several other organisms. The Gla-specific antibody used here provides a simple immunochemical means to detect gamma-carboxylated polypeptides in venom and may allow new species to be identified that utilize Gla in the biosynthesis of toxic polypeptides.
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3. |
- Dragani, B, et al.
(author)
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Role of conserved local motifs in folding and stability of hGSTP1-1
- 2001
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In: CHEMICO-BIOLOGICAL INTERACTIONS. - : ELSEVIER SCI IRELAND LTD. - 0009-2797. ; 133:1-3, s. 17-18
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Journal article (peer-reviewed)abstract
- We investigated, by site directed mutagenesis, the role played by a conserved N-capping box and hydrophobic staple motif in the folding and stability of human GSTPl-1. The corresponding mutants, I149A, S150A, D153A and Y154A, in which these motifs have be
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