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Glutamyl endopeptidase (EC 3.4.21.19, SspA, V8 protease, GluV8, endoproteinase Glu-C, staphylococcal serine proteinase) is an extracellular bacterial serine protease of the glutamyl endopeptidase I family that was initially isolated from the Staphylococcus aureus strain V8.
Endohydrolysis of (1→3)- or (1→4)-linkages in β-D-glucans when the glucose residue whose reducing group is involved in the linkage to be hydrolysed is itself substituted at C-3 Substrates include laminarin , lichenin and cereal D - glucans .
[8] It deglycosylates mannose glycoproteins, but the extent and rate of the deglycosylation depends to a high degree on the nature of the glycoproteins. The deglycosylation rate can be increased by denaturation of the glycoproteins (e.g., by carboxymethylation, sulfitolysis or by heating in the presence of sodium dodecyl sulfate).
β-Glucosidase is composed of two polypeptide chains. [3] Each chain is made up of 438 amino acids and constitute a subunit of the enzyme. [4] Each of these subunits contains an active site.
In enzymology, a xyloglucan-specific endo-beta-1,4-glucanase (EC 3.2.1.151) is an enzyme that catalyzes the chemical reaction. xyloglucan + H 2 O xyloglucan oligosaccharides. Thus, the two substrates of this enzyme are xyloglucan and H 2 O, whereas its product is xyloglucan oligosaccharides.
2010: Endo acquired generic manufacturer Qualitest Pharmaceuticals for $1.2 billion [8] 2011: Endo acquired medical device manufacturer American Medical Systems for more than $2 billion [18] [19] [7] 2013: Endo agreed to purchase Paladin Labs Inc for about $1.6 billion to gain access to the Canadian market as well as expand into emerging markets.
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It catalyses endohydrolysis of (1→4)-β-D-galactosidic linkages in keratan sulfate. It hydrolyses the 1,4-β- D -galactosyl linkages adjacent to 1,3- N -acetyl-α- D -glucosaminyl residues. References