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 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.
School of Biosciences, Hiroshima Prefectural University, Shobara City, Japan.
E
E
Hifumi
K
K
Ohara
Y
Y
Niimi
T
T
Uda
D000595:Amino Acid Sequence; D000818:Animals; D017151:Antibodies, Catalytic / Q000737:chemistry*; D000911:Antibodies, Monoclonal / Q000737:chemistry; D001666:Binding Sites, Antibody; D002614:Chelating Agents; D004492:Edetic Acid; D015483:HIV Antibodies / Q000737:chemistry*; D015700:HIV Envelope Protein gp41 / Q000235:genetics / Q000276:immunology; D006801:Humans; D007147:Immunoglobulin Light Chains / Q000737:chemistry; D066298:In Vitro Techniques; D051379:Mice; D008969:Molecular Sequence Data
D017151:Antibodies, Catalytic; D000911:Antibodies, Monoclonal; D002614:Chelating Agents; D015483:HIV Antibodies; D015700:HIV Envelope Protein gp41; D007147:Immunoglobulin Light Chains; D004492:Edetic Acid