Studies on human gastric mucosal cathepsin and its unique nature compared with other human pepsinogens
| Autor: | Jagdish C. Mangla, Gilda Guarasci, Michael D. Turner |
|---|---|
| Rok vydání: | 1974 |
| Předmět: |
Electrophoresis
Protein Denaturation Chromatography Paper Proteolysis Biochemistry Hemoglobins Column chromatography Pepsin Drug Stability Gastrectomy Gastric mucosa medicine Peptide bond Animals Humans Insulin Electrophoresis Paper Cathepsin chemistry.chemical_classification biology medicine.diagnostic_test Pepsinogens Chemistry Hydrogen-Ion Concentration Chromatography Ion Exchange Molecular biology Cathepsins Peptide Fragments Agar Kinetics medicine.anatomical_structure Enzyme Sephadex Gastric Mucosa biology.protein Chromatography Gel Cattle |
| Zdroj: | Biochemical medicine. 10(1) |
| ISSN: | 0006-2944 |
| Popis: | The material in human gastric mucosa known as cathepsin can be distinguished from the other proteinases by its low mobility on agar gel electrophoresis. It was shown to increase its mobility on acid activation. Sufficient enzyme was purified by phosphate gradient column chromatography on DEAE-cellulose, Sephadex G-100, and Pevikon block electrophoresis to allow study of some of its properties. The enzyme differs from the other human gastric proteinases by its resistance to destruction by alkali after acidification, by having a somewhat higher pH optimum for proteolysis, and by a different peptide bond specificity. The results indicate that the human gastric mucosa contains at least three distinct classes of acid proteinase which are capable of attacking different peptide bonds. |
| Databáze: | OpenAIRE |
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