L. Aldwin, D. Nitecki
Aug 1, 1987
Citations
0
Influential Citations
37
Citations
Journal
Analytical biochemistry
Abstract
A novel, freely water-soluble, heterobifunctional crosslinking reagent, N-maleimido-6-aminocaproyl ester of 1-hydroxy-2-nitro-4-benzenesulfonic acid (mal-sac-HNSA), was synthesized and used for conjugation of sulfhydryl (cysteine)-containing peptides to carrier proteins. Reaction with amino groups releases the dianion phenolate, HNSA, which allows convenient spectrophotometric quantitation of the reaction in progress. Since mal-sac-HNSA is completely water soluble, its concentration can be adjusted to maximize the rate of amine reaction and to minimize hydrolysis. Conjugates of peptides to appropriate carriers have elicited peptide-specific antibody and did not elicit detectable antibody specific to the crosslink.