Project description:Snake liver has been implicated in the adaptation of snakes to a variety of habitats. However, to date, there has been no systematic analysis of snake liver proteins. In this study, we undertook a proteomic analysis of liver from the colubrid snake Elaphe taeniura using a combination of two-dimensional electrophoresis (2-DE) and matrix-assisted laser desorption/ionization time of flightmass spectrometry (MALDI-TOF MS). We also constructed a local protein sequence database based on transcriptome sequencing to facilitate protein identification. Of the 268 protein spots revealed by 2-DE 109 gave positive MS signals, 84 of which were identified by searching the NCBInr, Swiss-Prot and local databases. The other 25 protein spots could not be identified, possibly because their transcripts were not be stable enough to be detected by transcriptome sequencing. GO analysis showed that most proteins may be involved in binding, catalysis, cellular processes and metabolic processes. Forty-two of the liver proteins identified were found in other reptiles and in amphibians. The findings of this study provide a good reference map of snake liver proteins that will be useful in molecular investigations of snake physiology and adaptation.
Project description:One of our previous studies has shown that there are two IgY subclasses (termed IgY1 and IgY2) in the serum of snake Elaphe taeniura, and both subclasses are expressed as full-length and shortened isoforms (IgY1-L, IgY2-L,IgY1-S, and IgY2-S). Using 2-DE and LC-MS/MS, we detected IgY1-L, IgY2-L,IgY1-S, IgY2-S, and the trunction (IgY-T), the LC-MS/MS results showed both IgY1and IgY2 were truncted at N338 of the heavy chain constant region.)