Epitopes described in "Antibody light chain-catalyzed hydrolysis of a hepatitis C virus peptide."

Reference
Article Authors:Hiroaki Taguchi; Zhenyong Keck; Steven K H Foung; Sudhir Paul; Yasuhiro Nishiyama
Article Title:Antibody light chain-catalyzed hydrolysis of a hepatitis C virus peptide.
Reference Detail
Reference ID:1001389
Abstract:A panel of human monoclonal and recombinant antibody light chains was screened for cleavage of the synthetic peptide corresponding to a neutralizing epitope of hepatitis C virus (residues 192-205 of envelope glycoprotein E1). One of the 39 light chains studied hydrolyzed the Val197-Ser198 bond of the peptide with Km and kcat values of 223 +/- 7 microM and 0.087 +/- 0.001 min(-1).
Affiliations:Chemical Immunology and Therapeutics Research Center, Department of Pathology and Laboratory Medicine, University of Texas-Houston Medical School, 6431 Fannin, 77030, USA.
Date:2004
Reference Type:Literature
PubMed ID:15357986
Journal:Bioorg Med Chem Lett
Journal Volume:14
Article Pages:4529-32
Journal ISSN:1464-3405
Article Chemical List:Antibodies, Monoclonal;Hepatitis C Antibodies;Immunoglobulin Light Chains;Peptide Fragments;Peptide Library;Recombinant Proteins;Viral Proteins
Article MeSH List:Antibodies, Monoclonal(metabolism); Catalysis; Hepacivirus(immunology; metabolism); Hepatitis C Antibodies(metabolism); Humans; Hydrolysis; Immunoglobulin Light Chains(metabolism); Peptide Fragments(immunology; metabolism); Peptide Library; Recombinant Proteins(metabolism); Viral Proteins(immunology; metabolism)
Curation Last Updated:2013-05-28 20:19:33