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Investigation of active form of catalytic antibody light chain 41S-2-L
- Source :
-
Immunology Letters . Jan2005, Vol. 96 Issue 1, p63-71. 9p. - Publication Year :
- 2005
-
Abstract
- Abstract: We have raised a monoclonal antibody (41S-2) against the conserved sequence, RGPDRPEGIEEEGGERDRD, of human immunodeficiency virus type1 (HIV-1) envelope gp41. That antibody light chain (41S-2-L) cleaves gp41-derived peptide (TPRGPDRPEGIEEEGGERDRD; TP41-1) with a characteristic biphasic profile composed of induction and active phases. It is considered that the conformation of 41S-2-L is changed, by such as induced fitting, to move to active phase to decompose the antigenic peptide during the induction phase. In order to investigate what happens to 41S-2-L in the induction and active phase, the cleavage reaction of the peptide by 41S-2-L was examined in detail from the viewpoint of kinetic and spectroscopic analysis. The kinetic data showed that the preferable conformational transition of 41S-2-L took place by the unimolecular reaction of 41S-2-L in the induction phase. UV–vis and fluorescence spectroscopic analysis suggested that the conformational transition leads to the generation of aggregates of 41S-2-L in the reacting solution, which causes the huge enhancement of the catalytic activity of 41S-2-L. The nuclei of the aggregates may be formed in the induction phase. The aggregates and soluble 41S-2-L are considered to be in chemical equilibrium during the cleavage reaction of the antigen. [Copyright &y& Elsevier]
- Subjects :
- *MONOCLONAL antibodies
*BLOOD plasma
*BLOOD proteins
*CHEMICAL reactions
*HIV
Subjects
Details
- Language :
- English
- ISSN :
- 01652478
- Volume :
- 96
- Issue :
- 1
- Database :
- Academic Search Index
- Journal :
- Immunology Letters
- Publication Type :
- Academic Journal
- Accession number :
- 15561570
- Full Text :
- https://doi.org/10.1016/j.imlet.2004.07.018