Titlebook: Structure and Function of the Aspartic Proteinases; Genetics, Structures Ben M. Dunn Book 1991 The Editor(s) (if applicable) and The Author

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Studies on Pepsin Mutagenesis and Recombinant Rhizopuspepsinogente of some diverse substrate specificities, these enzymes are alike in many ways, including their folding patterns, active center structures, and mechanisms of zymogen activation. Because the catalytic apparatuses of these enzymes are nearly identical, it is obvious that this group of enzymes shares

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Why Does Pepsin Have a Negative Charge at Very Low pH? An Analysis of Conserved Charged Residues in fferent substrates and a high activity at pH 2. This implies a very stable tertiary structure under conditions in which many proteins are fully denatured. These properties of pepsin are critical for its physiological function which takes place in the extreme acid conditions of the gastric lumen. The

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X-Ray Structural Studies of Mammalian Aspartic Proteinasescomponent of gastric juice in pigs, is produced by the mucosal cells of the fundus region of the stomach as an inactive precursor, pepsinogen. On secretion into the acidic lumen of the stomach, cleavage of the propart peptide occurs yielding active pepsin as a single chain molecule.

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Nonspecific Electrostatic Binding of Substrates and Inhibitors to Porcine Pepsin inhibitors (e.g., aliphatic alcohols) is also dominated by hydrophobic interactions.. However, the long standing ‘hydrophobic dogma’ in pepsin catalysis was seriously challenged when Pohl and Dunn. described a series of polycationic oligopeptides that are among the most reactive synthetic substrate

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Analysis of the Promoter of a Human Pepsinogen a Genemultigene family.. Electrophoretic separation of the PGA isozymogens from urine or gastric mucosa reveals three main fractions: Pg3, Pg4 and Pg5. The electrophoretic patterns of PGA show a large, genetically-determined, inter-individual heterogeneity. These differences can be explained by the presen

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