Abstract
From acid-disintegrated flagellar hooks of Salmonella SJ25 an immunochemically pure preparation of hook protein was obtained by column chromatography. The molecular weight of the protein determined by sodium dodecyl sulfate-gel electrophoresis was 43,000, whereas that of SJ25 flagellin was 56,000. The amino-terminal residue of the hook protein was determined to be seryl. The amino acid composition of the protein was determined, the results being very similar to that for an Escheria coli hook protein reported by Silverman and Simon (1972). Within a wavelength range of 200 to 250 nm, our purified preparation of hook protein gave a circular dichroism spectrum with unusually small amplitudes, suggesting that the alpha-helix content of the protein was very low.