Proton Magnetic Resonance of Proteins Fully Deuterated except for 1 H-Leucine Side Chains
Authors:
- 23 August 1968
- journal article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 161 (3843) , 795-796
Abstract
The fully deuterated proteins C-phycocyanin, C-phycoerythrin, and cytochrome c have been obtained by biosynthesis with the leucine side chains, and only the leucine side chains, of normal ( 1 H) isotopic composition. In these (isotopic hybrid) proteins, proton magnetic resonance analysis shows that the 1 H-leucine side chains are in a variety of environments. During protein biosynthesis, the alpha hydrogen of leucine is exchanged with a hydrogen ( 2 H) from the aqueous medium.Keywords
This publication has 6 references indexed in Scilit:
- Deuterated Organisms: Cultivation and UsesScience, 1966
- Association and Dissociation of Phycocyanin and the Effects of Deuterium Substitution on the Processes*Biochemistry, 1965
- Hydrogen Exchange at Carbon-Hydrogen Sites during Acid or Alkaline Treatment of ProteinsBiochemistry, 1964
- Mass cultivation of algae in pure heavy waterBiotechnology and Bioengineering, 1962
- Isolation of Fully Deuterated Metabolites from Scenedesmus obliquus Grown in Deuterium OxideJournal of Pharmaceutical Sciences, 1961
- Preparation and properties of three pure crystalline bacterial haem proteinsBiochimica et Biophysica Acta, 1961