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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Sun M,Paul Sdoi
10.1016/s0014-5793(97)00355-4subject
Has Abstractpub_date
1997-05-05 00:00:00pages
289-90issue
3eissn
0014-5793issn
1873-3468pii
S0014-5793(97)00355-4journal_volume
407pub_type
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