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In biochemistry, denaturation is a process in which proteins or nucleic acids lose folded structure present in their native state due to various factors, including application of some external stress or compound, such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), agitation and radiation, or heat. [3]
In 1926, James B. Sumner showed that the enzyme urease was a pure protein and crystallized it; he did likewise for the enzyme catalase in 1937. The conclusion that pure proteins can be enzymes was definitively demonstrated by John Howard Northrop and Wendell Meredith Stanley, who worked on the digestive enzymes pepsin (1930), trypsin and ...
The proteins elute according to their hydrophobicity. After purification by HPLC the protein is in a solution that only contains volatile compounds, and can easily be lyophilized. [11] HPLC purification frequently results in denaturation of the purified proteins and is thus not applicable to proteins that do not spontaneously refold.
The digestion-resistant maltodextrin ingredient has several properties exploited in food or beverage manufacturing: it is a low-moisture (5% water), free-flowing, fine white powder that disperses readily in water; it is clear in solution with low viscosity; it is odorless, slightly acidic, and has a bland flavor; it is 90% dietary fiber. [3]
In addition, in living systems, most biochemical reactions (including ATP hydrolysis) take place during the catalysis of enzymes. The catalytic action of enzymes allows the hydrolysis of proteins, fats, oils, and carbohydrates. As an example, one may consider proteases (enzymes that aid digestion by causing hydrolysis of peptide bonds in proteins).
An O-linked glycoprotein has the sugar is bonded to an oxygen atom of a serine or threonine amino acid in the protein. [ 4 ] Glycoprotein size and composition can vary largely, with carbohydrate composition ranges from 1% to 70% of the total mass of the glycoprotein. [ 4 ]
This polypeptide chain then goes through post translational modifications and is sometimes joined with other polypeptide chains to form a fully functional protein. Dietary proteins are first broken down to individual amino acids by various enzymes and hydrochloric acid present in the gastrointestinal tract. These amino acids are absorbed into ...
A standard enzyme preparation should be run in parallel with an unknown because standardization of DNA preparations and their degree of polymerization in solution is not possible. Single Radial Enzyme Diffusion (SRED) This simple method for DNase I activity measurement was introduced by Nadano et al. and is based on the digestion of DNA in the ...