Solubilization and properties of chloroplast lamellar protein.
- 1 November 1966
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 56 (5) , 1564-1570
- https://doi.org/10.1073/pnas.56.5.1564
Abstract
Most of the protein of chard and corn chloroplast lamellae and corn proplastids was solubilized by treatment with n-butanol at room temperature. No detergent was required to solubilize the proteins. The solubilized proteins interacted with large amounts of chloroplast lipid and chlorophyll, and tests with the chard protein showed that the protein could also interact with phospholipid and cyto-chrome. The amino acid compositions of all the proteins were remarkably similar.This publication has 20 references indexed in Scilit:
- Isolation and properties of a structural protein from chloroplastsBiochemical and Biophysical Research Communications, 1964
- Interactions of mitochondrial structural protein with phospholipidsArchives of Biochemistry and Biophysics, 1964
- Structure and function of subcellular particlesComparative Biochemistry and Physiology, 1962
- Physical Characteristics of Proteins of the Electron Transfer System and Interpretation of the Structure of the Mitochondrion*Biochemistry, 1962
- Partial purification and determination of oxidation reduction potential of the photosynthetic chlorophyll complex absorbing at 700 mμBiochimica et Biophysica Acta, 1961
- Automatic recording apparatus for use in the chromatography of amino acids.1958
- [Not Available].1956
- Crystalline chlorophyll and bacteriochlorophyllArchives of Biochemistry and Biophysics, 1954
- THE MECHANISM OF FORMATION OF CITRATE AND OXALATE BY ASPERGILLUS NIGERJournal of Biological Chemistry, 1952
- COPPER ENZYMES IN ISOLATED CHLOROPLASTS. POLYPHENOLOXIDASE IN BETA VULGARISPlant Physiology, 1949