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This paper describes evidence for hydrolysis of a neuropeptide, vasoactive intestinal peptide (VIP), by light chains purified from the IgG of a human subject positive for VIP binding antibodies. Purified IgG was digested with papain, resultant fragment antigen binding (Fab) fragments were reduced with 2-mercaptoethanol and alkylated with iodoacetamide, and light chains were purified by chromatography on immobilized antibodies to light chains and immobilized antibodies to heavy chains. Non-immunoglobulin components were undetectable in the light chain preparation, judged by sodium dodecyl sulfate-electrophoresis and Western blotting with anti-heavy and anti-light chain antibodies. The light chains hydrolyzed VIP with specific activity 32-fold greater than that of Fab, the pH optimum for light chain-mediated VIP hydrolysis was 7.0-7.5, and the hydrolytic activity was saturable (Vmax, 0.19 pmol/min/microgram light chains; substrate concentration at Vmax/2,380 nM).
S Mei, and
B Mody, and
S H Eklund, and
S Paul
June 1989,
Science (New York, N.Y.),
S Mei, and
B Mody, and
S H Eklund, and
S Paul
August 1996,
Biochimica et biophysica acta,
S Mei, and
B Mody, and
S H Eklund, and
S Paul
November 1994,
International journal of peptide and protein research,
S Mei, and
B Mody, and
S H Eklund, and
S Paul
June 1998,
Doklady Akademii nauk,
S Mei, and
B Mody, and
S H Eklund, and
S Paul
April 1986,
Journal of endocrinological investigation,
S Mei, and
B Mody, and
S H Eklund, and
S Paul
July 1990,
The Journal of biological chemistry,
S Mei, and
B Mody, and
S H Eklund, and
S Paul
January 2005,
Methods in enzymology,
S Mei, and
B Mody, and
S H Eklund, and
S Paul
January 1978,
Journal of clinical pathology. Supplement (Association of Clinical Pathologists),
S Mei, and
B Mody, and
S H Eklund, and
S Paul
May 1998,
The Journal of pharmacology and experimental therapeutics,
S Mei, and
B Mody, and
S H Eklund, and
S Paul
September 1982,
The American journal of physiology,
