Electrophoretic characterization of human, equine and bovine transferrins

1. Human, bovine and equine transferrins have been characterized with respect to mol. wt, and behavior on urea-polyacrylamide gels, and isoelectric focussing gels. 2. As shown by SDS-polyacrylamide gel electrophoresis human transferrin has one major polypeptide whereas both bovine and equine transferrins have two polypeptides. 3. The transferrins show multiple banded patterns on urea-polyacrylamide and isoelectric focussing gels, particularly when iron saturated. The various forms are not resolved by neuraminidase treatment.     

Correlates of substitution rate variation in mammalian protein-coding sequences

Background  

Rates of molecular evolution in different lineages can vary widely, and some of this variation might be predictable from aspects of species' biology. Investigating such predictable rate variation can help us to understand the causes of molecular evolution, and could also help to improve molecular dating methods. Here we present a comprehensive study of the life history correlates of substitution rate variation across the mammals, comparing results for mitochondrial and nuclear loci, and for synonymous and non-synonymous sites. We use phylogenetic comparative methods, refined to take into account the special nature of substitution rate data. Particular attention is paid to the widespread correlations between the components of mammalian life history, which can complicate the interpretation of results.