[Proteome Analysis for Identification of the Origin of Biological Foreign Substances].

We have developed a method for determination of the species of origin of biological foreign substances using proteomics analysis technology. That is, the amino acid sequence of the tryptic digested product of the protein extracted from the foreign substance is determined by high-resolution LC-MS, and the amino acid sequence is collated with a public protein database to determine the origin species of the foreign substance. As a result of testing meat (beef, pork, chicken) and egg (chicken, quail) from known origin as simulated foreign substances, we were able to find species-specific amino acid sequences for each species, suggesting that the developed method is useful for species discrimination of a foreign substances that have been heat-treated with retort, this method is potentially useful to complement DNA analysis, for determination of the species of origin of foreign substances.

Copper binding selectivity of N- and C-sites in serum (human)- and ovo-transferrin.

Copper binding selectivity of the N- and C-sites in serum (human)- and ovo-transferrin was investigated through copper binding constants, copper dissociation rate constants, and EPR spectra. At pH 7.4, stepwise copper binding constants of serum (human)-transferrin were K1 = 1.