Removal of catalytic activity by EDTA from antibody light chain

Gp41 peptide antigen of the HIV-1 envelope (TP41-1:TPRGPDRPEGIEEEGGERDR, a highly conserved region) was enzymatically degraded by the antibody light chain 41S-2-L after an induction period. The peptide bond between Glu14 and Gly15 was cleaved early in the reaction. When EDTA was added in the inducti...

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Bibliographic Details
Published in:Biometals 2000-12, Vol.13 (4), p.289-294
Main Authors: Hifumi, E, Ohara, K, Niimi, Y, Uda, T
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Antibodies
Antibodies, Catalytic - chemistry
Antibodies, Monoclonal - chemistry
Antigens
Binding Sites, Antibody
Biodegradation
Bonding
Catalysis
Catalytic activity
Chains
Chelating Agents
Chemical reactions
Degradation
Edetic Acid
EDTA
Enzymes
HIV Antibodies - chemistry
HIV Envelope Protein gp41 - genetics
HIV Envelope Protein gp41 - immunology
Humans
Immunoglobulin Light Chains - chemistry
In Vitro Techniques
Metal ions
Mice
Molecular Sequence Data
Peptides
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Summary:Gp41 peptide antigen of the HIV-1 envelope (TP41-1:TPRGPDRPEGIEEEGGERDR, a highly conserved region) was enzymatically degraded by the antibody light chain 41S-2-L after an induction period. The peptide bond between Glu14 and Gly15 was cleaved early in the reaction. When EDTA was added in the induction period, it inhibited the degradation of TP41-1 thus ceasing the catalytic activity of 41S-2-L. In contrast, when EDTA was added after the induction period, only a small reduction in the catalytic activity was observed. These observations suggest that metal ions are important in stimulating catalytic activity early in the reaction.
ISSN:0966-0844
1572-8773
DOI:10.1023/a:1009252200231