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Altered cleavage site preference of a proteolytic antibody light chain induced by denaturation

Authors
Journal
FEBS Letters
0014-5793
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Volume
407
Issue
3
Identifiers
DOI: 10.1016/s0014-5793(97)00355-4
Keywords
  • Catalytic Antibody
  • Substrate Specificity
  • Antibody Engineering
Disciplines
  • Biology

Abstract

Abstract A recombinant antibody light chain (L chain) maintained under non-denaturing conditions displayed preferential cleavage of synthetic peptides conjugated to methylcoumarinamide (MCA) on the C-terminal side of Arg and Lys residues. The same L chain renatured from a denaturing solvent (guanidine hydrochloride) acquired the capability of cleaving Tyr–MCA and Leu–MCA bonds, and its ability to cleave MCA linked to basic residues was decreased. The altered cleavage preference was accompanied by a conformational transition in the protein, evident from the fluorescence emission spectra. These observations suggest the feasibility of redirecting the cleavage specificity via alterations in the conformation of proteolytic antibody combining sites.

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