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

FEBS Letters

Paul, Sudhir¹  Sun, Mei¹ 

[1] University of Nebraska Medical Center, Department of Anesthesiology and Eppley Cancer Research Institute, Omaha, NE 68198-6830, USA

关键词: Catalytic antibody;    Substrate specificity;    Antibody engineering;   

DOI  :  10.1016/S0014-5793(97)00355-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown