NDLI: Removal of catalytic activity by EDTA from antibody light chain

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Removal of catalytic activity by EDTA from antibody light chain

Content Provider	Springer Nature Link
Author	Hifumi, Emi Ohara, Kyoko Niimi, Yoshiyuki Uda, Taizo
Copyright Year	2000
Abstract	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.
Starting Page	289
Ending Page	294
Page Count	6
File Format	PDF
ISSN	09660844
Journal	BioMetals
Volume Number	13
Issue Number	4
e-ISSN	15728773
Language	English
Publisher	Kluwer Academic Publishers
Publisher Date	2000-01-01
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Physical Chemistry Biochemistry
Content Type	Text
Resource Type	Article
Subject	Metals and Alloys Biochemistry, Genetics and Molecular Biology Biomaterials Agricultural and Biological Sciences

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