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In practice, a protein with an excess of basic aminoacids (arginine, lysine and/or histidine) will bear an isoelectric point roughly greater than 7 (basic), while a protein with an excess of acidic aminoacids (aspartic acid and/or glutamic acid) will often have an isoelectric point lower than 7 (acidic).
It was first defined by S.P.L. Sørensen, Kaj Ulrik Linderstrøm-Lang and Ellen Lund in 1926 [1] and is mainly a term used in protein sciences. It is different from the isoelectric point (pI) in that pI is the pH value at which the net charge of the molecule, including bound ions is zero. Whereas the isoionic point is at net charge zero in a ...
Bovine serum albumin (BSA or "Fraction V") is a serum albumin protein derived from cows. It is often used as a protein concentration standard in lab experiments. The nickname "Fraction V" refers to albumin being the fifth fraction of the original Edwin Cohn purification methodology that made use of differential solubility characteristics of plasma proteins.
The words protein, polypeptide, and peptide are a little ambiguous and can overlap in meaning. Protein is generally used to refer to the complete biological molecule in a stable conformation, whereas peptide is generally reserved for a short amino acid oligomers often lacking a stable 3D structure. But the boundary between the two is not well ...
The isoelectric point of albumin is 4.7. [8] Alpha-fetoprotein is a fetal plasma protein that binds various cations, fatty acids and bilirubin. Vitamin D-binding protein binds to vitamin D and its metabolites, as well as to fatty acids. Not much is known about afamin. It seems to carry lipidated Wnt proteins and Vitamin E around. [9]
[72] [73] [74] The isoelectric point of a given molecule is a function of its pK values, so different molecules have different isoelectric points. This permits a technique called isoelectric focusing , [ 75 ] which is used for separation of proteins by 2-D gel polyacrylamide gel electrophoresis .
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 ...
[1] [2] They are water soluble low-molecular weight basic proteins classified as 2S or 1.7S proteins, representing 20–40% of total seed protein, and having a molecular weight in the range of 12–17 kDa. [3] [4] Their isoelectric point varies based on the method of extraction and the specific characteristics of the isoforms that exist. They ...