Immobilized-metal-ion affinity chromatography as a tool for the qualitative study of pepsinogen phosphorylation
Language English Country Netherlands Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
11694299
DOI
10.1016/s0165-022x(01)00217-2
PII: S0165022X01002172
Knihovny.cz E-resources
- MeSH
- Chromatography, Affinity methods MeSH
- Chromatography, Ion Exchange methods MeSH
- Phosphorylation MeSH
- Chromatography, Gel methods MeSH
- Indicators and Reagents MeSH
- Metals MeSH
- Humans MeSH
- Ligands MeSH
- Oligopeptides MeSH
- Pepsin A metabolism MeSH
- Pepsinogen A metabolism MeSH
- Buffers MeSH
- Amino Acid Sequence MeSH
- Gastric Mucosa enzymology MeSH
- Ferric Compounds MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Indicators and Reagents MeSH
- Metals MeSH
- Ligands MeSH
- Oligopeptides MeSH
- Pepsin A MeSH
- Pepsinogen A MeSH
- Buffers MeSH
- Ferric Compounds MeSH
Affinity chromatography on immobilized Fe(3+) ions--immobilized-metal-ion affinity chromatography (IMAC) method--was used for the determination of pepsin and pepsinogen phosphorylation. IMAC is a very powerful method for detailed studies of proteins. Dephosphorylation of the pepsinogens and pepsins has no effect on their proteolytic ability. For this reason, the determination of proteolytic activity was used for the detection of pepsinogen (pepsin) presence in the collected fractions as a very suitable and specific method. Pepsins and their zymogens probably have the same amounts of phosphate ions in their molecule. The exact definition of conditions is very important for the prepurification of the proteinases and for their analysis.
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