Asian-Pacific Aquaculture 2019

June 19 - 21, 2019

Chennai Tamil Nadu - India

ASSESSMENT OF PROTEIN FINGERPRINTING ON SODIUM DODECYL SULPHATE - POLYACRYLAMIDE GEL (SDS - PAGE) FOR LOACH SPECIES

V. Kaliyamurthi*, Ambika Binesh and K. Karal Marx
Institute of Fisheries Post Graduate Studies
TNJFU-OMR Campus
Vaniyanchavadi, Chennai - 603 103
 
kaliyamurthi@tnfu.ac.in
 

Proteins are made up of amino acid chain. Isoelectric focussing, 2 D gel electrophoresis, immunoblotting, autoradiography, mass spectrometry and SDS-PAGE are widely used to identify specific proteins and their diversity. SDS-PAGE stands for sodium dodecyl sulphate - polyacrylamide gel electrophoresis. Generally, a gel is used to identify protein or DNA, by separation of bands in each sample's specific lane. SDS-PAGE separate proteins based on their mass, the high molecular weight at the top and the low molecular weight on the bottom of its gel lane. Universally, protein is used to refer as complete biological molecule of any organism. Thus, the degree of relatedness of the two species can be estimated from the amount and expression of similarity between their protein makeups. The aim of the study was to investigate the protein profile pattern of three Indian loach species namely Lepidocephalus thermalis, Botia lohachata and Botia ghetto by SDS-PAGE. Protein was extracted from three different species of whole loach and compared by using 10% polyacrylamide gel electrophoresis.  

The individual bands were corresponding to different proteins and varied in expression pattern between species. In addition, some bands (i.e., proteins) visible in one species fingerprint but not in another. In general, protein fingerprint patterns obtained from different species are more similar when the species are more closely related and less similar when they are more distantly related. In this study, we observed differential expression pattern of proteins in three species (indicated by arrow head in Figure 1). To study further, the differently expressed protein will be characterised by LC-MS/MS studies and the spectral data will be utilised to identify the specific protein.