Simultaneous incorporation of 18O into succinate and hydroxyproline catalyzed by collagen proline hydroxylase
| Autor: | Robert E. Rhoads, George J. Cardinale, Sidney Udenfriend |
|---|---|
| Rok vydání: | 1971 |
| Předmět: |
Chromatography
Gas Chemical Phenomena Proline Stereochemistry Decarboxylation Biophysics Oxygen Isotopes Models Biological Biochemistry Mass Spectrometry Mixed Function Oxygenases Catalysis chemistry.chemical_compound Hydroxyproline Animals Molecular Biology Skin chemistry.chemical_classification Carbon Isotopes biology Succinates Cell Biology Catalase Chromatography Ion Exchange Rats Oxygen Chemistry Enzyme Animals Newborn Liver chemistry Succinic acid biology.protein Ketoglutaric Acids Cattle Peptides Oxidation-Reduction Mathematics |
| Zdroj: | Biochemical and Biophysical Research Communications. 43:537-543 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/0006-291x(71)90647-4 |
| Popis: | The sequential copolymer (Pro-Gly-Pro)∼12 was hydroxylated in an 18O2 atmosphere with a partially purified preparation of collagen proline hydroxylase. Mass spectral analysis demonstrated the incorporation of one atom of 18O into hydroxyproline and one atom into succinic acid. Since the enzyme produces equal amounts of peptidyl hydroxyproline and succinate these findings strongly suggest that one molecule of O2 takes part in the simultaneous oxygenation of peptidyl proline and α-keto-glutarate. A possible mechanism for this reaction is presented. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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