Abstract
The alkaline phosphatase activities of five unique isolates of marine bacteria were found to be associated with the periplasmic space; however, the enzymes from these isolates differed with respect to their repressibility, the apparent number of isoenzymes, the necessity for Mg2 for activity, and the conditions required for their release. With three of the isolates, the enzyme was released when cells that had been washed in 0.5 M NaCl were suspended in sucrose; however, with the other two isolates, one required the additional presence of tris(hydroxymethyl)aminomethane and the other required the presence of lysozyme and ethylenediaminetetraacetic acid. In two isolates the activity was constitutive, in two it was partially repressed, and in one it was completely repressed by inorganic phosphate. The repression of activity was associated with corresponding changes of activity bands as seen by acrylamide gel electrophoresis.