Abstract
The purified protein which constitutes the membranes of the gas vacuoles of the the blue-green alga, Microcystis aeruginosa, was partially characterized. Gel electrophoresis and end-group analysis indicate that the protein is a single species. Strongly protic solvents such as formic acid are the only reagents causing appreciable solubilization of the membrane protein. Infrared spectroscopy shows that the membrane protein has both α-helix or random-coil conformation, and β-conformation.