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The isoelectric point (pI, pH(I), IEP), is the pH at which a molecule carries no net electrical charge or is electrically neutral in the statistical mean. The standard nomenclature to represent the isoelectric point is pH(I). [1] However, pI is also used. [2] For brevity, this article uses pI.
The isoelectric point is the pH at which a compound - in this case a protein - has no net charge. A protein's isoelectric point or PI can be determined using the pKa of the side chains, if the amino (positive chain) is able to cancel out the carboxyl (negative) chain, the protein would be at its PI.
For this reason isoelectric point precipitation is most often used to precipitate contaminant proteins, rather than the target protein. The precipitation of casein during cheesemaking, or during production of sodium caseinate, is an isoelectric precipitation.
The two dimensions that proteins are separated into using this technique can be isoelectric point, protein complex mass in the native state, or protein mass. [citation needed] The separation by isoelectric point is called isoelectric focusing. Thereby, a pH gradient is applied to a gel and an electric potential is applied across the gel, making ...
The LRRN3 protein is 708 amino acids in length. The molecular weight of this protein is 79,424 daltons, with an isoelectric point of 8.02. [9] It is known to be a single-pass type I membrane protein because it spans the membrane once, with its N-terminus on the extracellular side of the membrane, and its signal sequence is removed.
Isoelectric focusing (IEF), also known as electrofocusing, is a technique for separating different charged molecules by differences in their isoelectric point (pI). [ 1 ] [ 2 ] It is a type of zone electrophoresis usually performed on proteins in a gel that takes advantage of the fact that overall charge on the molecule of interest is a ...
The three samples are mixed and loaded onto IEF (isoelectric focusing chromatography) for first dimension and the strip is transferred to a SDS PAGE.After the gel electrophoresis, the gel is scanned with the excitation wavelength of each dye one after the other, so each sample can be seen separately (if we scan the gel at the excitation wavelength of the Cy3 dye, we will see in the gel only ...
It is a byproduct of the manufacturing of cheese or casein and has several commercial uses. Sweet whey is a byproduct resulting from the manufacture of rennet types of hard cheese, like cheddar or Swiss cheese. Acid whey (also known as sour whey) is a byproduct brought out during the making of acid types of dairy products, such as strained yogurt.