Open AccessC 55 -Isoprenoid Alcohol Phosphokinase: An Extremely Hydrophobic Protein from the Bacterial Membrane
Author(s) -
Heinrich Sandermann,
Jack L. Strominger
Publication year - 1971
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.68.10.2441
Subject(s) - chemistry , sodium dodecyl sulfate , sodium , enzyme , polyacrylamide gel electrophoresis , butanol , chromatography , biochemistry , alcohol , amino acid , polyacrylamide , gel electrophoresis , membrane , organic chemistry , ethanol , polymer chemistry
C55 -isoprenoid alcohol phosphokinase, a butanol-soluble enzyme from the membrane ofStaphylococcus aureus , has been purified to homogeneity by the inclusion of organic solvents in all of the techniques used. By polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate, the enzyme is a single polypeptide chain of molecular weight 17,000. The amino-acid analysis reveals an unusually high content of nonpolar amino acids (58%), the largest amount so far reported in any protein. When equilibrated in butanol-water, enzyme apoprotein is found in the butanol layer. The influence of sodium chloride indicates that the lipid requirement of the enzyme is nonelectrostatic in nature.