Date of Defense
Summer 8-1980
Department
Biological Sciences
First Advisor
Robert C. Eisenberg
Second Advisor
M.E. McCarville
Third Advisor
J.L. Foote
Abstract
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.
Recommended Citation
Wolff, Joseph A., "Purification and Characterization of Mannitol Binding Protein in Pseudomonas Aeruginosa" (1980). Honors Theses. 199.
https://scholarworks.wmich.edu/honors_theses/199
Access Setting
Honors Thesis-Campus Only