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ABSTRACT:
SUBMITTER: Sapparapu G
PROVIDER: S-EPMC3476277 | biostudies-literature | 2012 Oct
REPOSITORIES: biostudies-literature
Sapparapu Gopal G Planque Stephanie S Mitsuda Yukie Y McLean Gary G Nishiyama Yasuhiro Y Paul Sudhir S
The Journal of biological chemistry 20120904 43
Some antibodies contain variable (V) domain catalytic sites. We report the superior amide and peptide bond-hydrolyzing activity of the same heavy and light chain V domains expressed in the IgM constant domain scaffold compared with the IgG scaffold. The superior catalytic activity of recombinant IgM was evident using two substrates, a small model peptide that is hydrolyzed without involvement of high affinity epitope binding, and HIV gp120, which is recognized specifically by noncovalent means p ...[more]