It’s time I put in a new avvie, so say hello to my new one!
I know it’s been a long time since I posted, but these exams are killing me. And this post here hasn’t got much to do with the blog, but I wanted to put it up anyway; It’s our (Mine and Amrutha’s) first ever SDS-PAGE gel, which has come out brilliantly! It is our 12th standard biotechnology project.
• So, about SDS-PAGE, it stands for Sodium Dodecyl Sulphate- Polyacrylamide Gel Electrophoresis.
• It is basically used to separate the different sub-units present in protein, and is also used in analyzing the components of a protein, the molecular weight and so on.
• We thank Santhi Ma’am (our biotech teacher, who is extremely sweet!) for telling us to do this!!
• Anyways, besides that, we electrophoresed 2 proteins-
o A standard sample of Bovine Serum Albumin
o Protein extract from mung beans.
• The proteins are denatured using SDS and boiling them. They are subject to an electric field and this causes them to move toward the anode as SDS gives the proteins a uniform negative charge.
• They are separated based on their molecular weights, the heavies moving the least, the lightest moving the fastest.
• These are your basic principles, and if you want more info, this isn’t the place to look, but if it’s nice pics, welcome aboard! Click on them for larger images 😉
• In this picture, the first two lanes and the last two lanes show the characteristic bands of standard (5%) BSA (bovine serum albumin).
• The middle 3 lanes are that of mung bean protein extract.
• Thicker bands => greater concentration of that subunit
• We used Coomassie Brilliant Blue (yes, it does sound funny!) to stain the proteins, tracker dye used – Bromophenol Blue
• This shows the gel after electrophoresis is complete, but it hasn’t been stained yet to view the protein bands.
This post is long due, we thought of putting it up in the December holz, but since we didn’t have any… *sigh*