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The Hopkins-Cole reaction, also known as the glyoxylic acid reaction, is a chemical test used for detecting the presence of tryptophan in proteins. [1] A protein solution is mixed with Hopkins Cole reagent, which consists of glyoxylic acid. Concentrated sulfuric acid is slowly added to form two layers. A purple ring appears between the two ...
This acetate, bound to the active thiol group of coenzyme A, enters the citric acid cycle (TCA cycle) where it is fully oxidized to carbon dioxide. This pathway thus allows cells to obtain energy from fat. To use acetate from fat for biosynthesis of carbohydrates, the glyoxylate cycle, whose initial reactions are identical to the TCA cycle, is ...
Glyoxylic acid is one of several ketone- and aldehyde-containing carboxylic acids that together are abundant in secondary organic aerosols. In the presence of water and sunlight, glyoxylic acid can undergo photochemical oxidation. Several different reaction pathways can ensue, leading to various other carboxylic acid and aldehyde products. [31]
It is a spontaneous reaction and a type of post-translational modification of proteins meaning it alters their structure and biological activity. It is the covalent attachment between the carbonil group of a reducing sugar (mainly glucose and fructose) and the amino acid side chain of the protein. In this process the intervention of an enzyme ...
The reaction relies on the interaction between glyoxylic acid and the indole ring of the amino acid tryptophan, a structural feature found in most proteins. When proteins are exposed to concentrated sulfuric acid and glyoxylic acid, the indole group undergoes a reaction that produces a highly colored compound.
Calcium-binding proteins have specific domains that bind to calcium and are known to be heterogeneous. One of the functions of calcium binding proteins is to regulate the amount of free (unbound) Ca 2+ in the cytosol of the cell. [1] The cellular regulation of calcium is known as calcium homeostasis.
In enzymology, a glycine dehydrogenase (EC 1.4.1.10) is an enzyme that catalyzes the chemical reaction glycine + H 2 O + NAD + ⇌ {\displaystyle \rightleftharpoons } glyoxylate + NH 3 + NADH + H + The 3 substrates of this enzyme are glycine , H 2 O , and NAD + , whereas its 4 products are glyoxylate , NH 3 , NADH , and H + .
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 ]