Date of Defense
Robert C. Eisenberg
Mannitol binding protein (MBP) from Pseudomonas aeruginosa, strain PAO, was extracted and purified although not to homogeneity. Maximum stability of the protein activity at 4°C was attained using a citrate-phosphate buffer at pH 5.0. The approximate molecular weight was confirmed to be ca 36,000 daltons. Evidence for the periplasmic character of MBP was also obtained by adapting a spheroplast coldshock procedure originally developed for preparing membrane vesicles from P. aeruginosa. A comparison of the relative distribution of MBP to glucose-6-phosphate dehydrogenase in periplasmic, cytoplasmic and membrane fractions established that MBP is a periplasmic constituent of P. aeruginosa.
Wolff, Joseph A., "Purification and Characterization of Mannitol Binding Protein in Pseudomonas Aeruginosa" (1980). Honors Theses. 199.
Honors Thesis-Campus Only