Anti-Lysine Acetylated monoclonal antibody, clone 8G9

An extraordinary micro-structural similarity between squid sucker teeth and the egg shell of a terrestrial planarian worm has been reported, but to date only the amino acid content of the squid sucker tooth has been available. This prompted us to analyse the amino acid content of the planarian egg shell. Although both share an absence of detectable chitin and metal ions and both possess relatively high amounts of the amino acids GLY and HIS, the planarian egg shell is considerably richer in GLU, LYS and ASP. Most dramatic was the difference in TYR, which was the second most abundant amino acid in the squid, but hardly featured at all in the planarian egg shell. In the light of these new findings the different functional roles that the structures in question play in the lives of the two taxa are discussed. An EDS-analysis revealed clear C, N, and O peaks and additional very small peaks less than 0.1w% suggesting the presence of one or both S and Cl.

The conjugate prepared from (-)-epigallocatechin gallate (EGCG) and soy protein isolate (SPI) under alkaline and aerobic conditions was analyzed using a Nano-LC-Q-Orbitrap-MS/MS technique. The sulfhydryl and free amino groups of SPI were involved in covalent binding. Fifty-one peptides were conjugated with EGCG. Fifty-nine modified sites were identified, located on Cys, His, Arg, and Lys, respectively. It is the first time to confirm that each of the two phenolic rings of EGCG contained a reactive site that bound to an amino acid residue. The amino acid residue reactivity, amino acid sequence and composition affected the EGCG binding site in SPI. Lys and Arg residues are the most likely sites for modification, and modification appears to reduce IgE binding. This study is helpful to elucidate the pattern of covalent binding of polyphenols to proteins in food systems and provides a theoretical basis for the directional modification of soy proteins with polyphenols.