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

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 Lett

journal_title

FEBS letters

authors

Sun M,Paul S

doi

10.1016/s0014-5793(97)00355-4

subject

Has Abstract

pub_date

1997-05-05 00:00:00

pages

289-90

issue

3

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(97)00355-4

journal_volume

407

pub_type

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