@article{ref1,
title="Part 4: Evidence That Lethal Toxin Neutralizing Peptide Lt-10 Binds to Proteins and an Exploration of Its Potential Use in the in Vitro Assay of Toxins",
journal="Toxin reviews",
year="2008",
author="Lipps, Binie Ver",
volume="27",
number="2",
pages="125-125",
abstract="Natural lethal toxin neutralizing factor (N-LTNF), molecular weight 63.0 kDa, was isolated from opossum serum. After trypsin digestion, the active domain of N-LTNF was isolated and sequenced. A synthetic peptide consisting of 10 amino acids from the N-LTNF was designated as LT-10. N-LTNF and LT-10 inhibited the lethality of toxins from animals, plants, and bacteria when tested in mice by a non-immunological mechanism. However, the antibodies against N-LTNF and LT-10 reacted immunologically with toxins only and not with nontoxic substances. Anti-LTNF and anti-LT-10 detected toxins in an ELISA assay that were not detected by a mouse toxicity test, including cholera toxin and digoxin. Furthermore, anti-N-LTNF and anti-LT-10 failed to react immunologically with nontoxic substances, nerve growth factor and collagen. Currently, the mouse bioassay is standard practice for detection and assay of toxins. Binding affinity of anti-LT-10, measured as the ELISA detection limit, showed a linear relationship with the mouse bioassay. In addition, anti-LT-10 detects toxins that are not lethal to mice. Thus, anti-LT-10 may prove useful in assaying toxins as an alternative to mouse bioassay.<p />",
language="",
issn="1556-9543",
doi="10.1080/15569540802129748",
url="http://dx.doi.org/10.1080/15569540802129748"
}