Author Correction: Ancient DNA of Guinea Pigs (Cavia spp.) Indicates a Probable New Center of Domestication and Pathways of Global Distribution.

An amendment to this paper has been published and can be accessed via a link at the top of the paper.

Ancient DNA of Guinea Pigs (Cavia spp.) Indicates a Probable New Center of Domestication and Pathways of Global Distribution.

Guinea pigs (Cavia spp.) have a long association with humans. From as early as 10,000 years ago they were a wild food source. Later, domesticated Cavia porcellus were dispersed well beyond their native range through pre-Columbian exchange networks and, more recently, widely across the globe. Here we present 46 complete mitogenomes of archaeological guinea pigs from sites in Peru, Bolivia, Colombia, the Caribbean, Belgium and the United States to elucidate their evolutionary history, origins and paths of dispersal. Our results indicate an independent centre of domestication of Cavia in the eastern Colombian Highlands. We identify a Peruvian origin for the initial introduction of domesticated guinea pigs (Cavia porcellus) beyond South America into the Caribbean. We also demonstrate that Peru was the probable source of the earliest known guinea pigs transported, as part of the exotic pet trade, to both Europe and the southeastern United States. Finally, we identify a modern reintroduction of guinea pigs to Puerto Rico, where local inhabitants use them for food. This research demonstrates that the natural and cultural history of guinea pigs is more complex than previously known and has implications for other studies regarding regional to global-scale studies of mammal domestication, translocation, and distribution.

Model systems for oxidative drug metabolism studies. Catalytic behavior of water-soluble metalloporphyrins depends on both the intrinsic robustness of the catalyst and the nature of substrates.

Sulfonated manganese and iron porphyrins have been used as catalysts in attempts to mimick the oxidation of acetaminophen and two ellipticine derivatives by horseradish peroxidase. Cofactors were potassium monopersulfate for the synthetic catalyst and hydrogen peroxide for the natural enzyme. Hindered metalloporphyrins, i.e. with ortho positions of the meso-phenyl rings substituted with methyl groups [iron(III) and manganese(III) derivatives of octasodium mesotetrakis(3,5-disulfonatomesityl)porphyrin], were shown to be at least 10 times more robust than unsubstituted derivatives [iron(III) and manganese(III) derivatives of tetrasodium meso-tetrakis(4-sulfonatophenyl)porphyrin] when activated in the absence of substrate. The catalytic activity depends on the nature of the substrate as shown by a decrease or an increase in reactivity observed, respectively, in the oxidation of acetaminophen or ellipticine derivatives catalyzed by hindered metalloporphyrins compared with nonhindered ones. Only sterically hindered metalloporphyrins, even in the case of lowered reactivity, were allowed to mimick the behavior of horseradish peroxidase when activated in the absence of substrate (stability toward autodegradation) and in the course of repeated infusion of substrate (retained catalytic activity as time advances).