Inhibition of Human Pepsin and Gastricsin by α2-Macroglobulin
| Autor: | Masaaki Nishigai, Senarath B. P. Athauda, Atsushi Ikai, Kenji Takahashi, Masanori Ukai, Hideo Arakawa |
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| Rok vydání: | 2003 |
| Předmět: |
Time Factors
Protein Conformation medicine.medical_treatment Pepsin Drug Discovery medicine Aspartic Acid Endopeptidases Humans Histidine Protease Inhibitors alpha-Macroglobulins Ribonuclease Chromatography High Pressure Liquid Pharmacology chemistry.chemical_classification Alanine biology Insulin Native Polyacrylamide Gel Electrophoresis Substrate (chemistry) Valine General Medicine Hydrogen-Ion Concentration Gastricsin Molecular biology Pepsin A Macroglobulin Microscopy Electron Enzyme chemistry Biochemistry biology.protein Electrophoresis Polyacrylamide Gel Peptides Protein Binding |
| Zdroj: | Journal of Enzyme Inhibition and Medicinal Chemistry. 18:219-224 |
| ISSN: | 1475-6374 1475-6366 |
| DOI: | 10.1080/1475636031000101246 |
| Popis: | The inhibitory effects of human alpha2-macroglobulin (alpha2-M), a major plasma proteinase inhibitor, on human pepsin and gastricsin were investigated. The activities of pepsin and gastricsin towards a protein substrate (reduced and carboxymethylated ribonuclease A) were significantly inhibited by alpha2-M at pH 5.5, whereas those towards a peptide substrate (oxidized insulin B-chain) were scarcely inhibited. Under these conditions at pH 5.5, pepsin and gastricsin cleaved alpha2-M mainly at the His694-Ala695 bond and Leu697-Val698 bond, respectively, in the bait regions sequence of alpha2-M. The conformation of alpha2-M was also shown to be markedly altered upon inhibition of these enzymes as examined by native polyacrylamide gel electrophoresis and electron microscopy. These results show the entrapment and concomitant inhibition of those proteinases by alpha2-M. |
| Databáze: | OpenAIRE |
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