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The Journal of Immunology, Vol 153, Issue 11 5121-5126, Copyright © 1994 by American Association of Immunologists

ARTICLES

Proteolytic activity of an antibody light chain

M Sun, QS Gao, L Li and S Paul
Department of Anesthesiology, University of Nebraska Medical Center, Omaha 68198.

The light chain (L chain) of a mAb raised against unactivated vasoactive intestinal peptide (VIP) hydrolyzed this peptide, whereas the heavy chain (H chain) and an irrelevant L chain were without activity. The reaction kinetics were consistent with efficient substrate recognition by the anti-VIP L chain compared with conventional proteases. The L chain cleaved four peptide bonds clustered between residues 16 and 21 in VIP. Mixtures of the L chain with its H chain partner displayed reduced hydrolytic activity compared with the free L chain, suggesting that the H chain is a modulator of the catalytic activity. These observations suggest: 1) the immune system can generate catalytic sites in the L chain subunit of Abs found in response to polypeptide Ags, and 2) free L chains found in vivo could display an Ag-specific catalytic function.


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