Polysphondylium pallidum

A highly purified FDPase from the slime mold Polysphondylium pallidum has been shown (92), to hydrolyze both FDP and SDP, at nearly equal rates, to yield fructose 6-phosphate and sedoheptulose 7-phosphate, respectively. In other respects the purified enzyme was remarkably similar to that isolated from Candida utilis it was completely inactive at pH 7.5 or 8.0, and showed a pH optimum at 9.2. In the presence of low concentrations of EDTA a second pH optimum appeared at pH 7.5. Unlike the Candida FDPase, however, the Polysphondylium enzyme was not inhibited by AMP at any pH. The levels of enzyme which could be extracted from the cells did not change significantly during the various stages of differentiation, and its activity could not be related to catabolic or anabolic processes which characterize these stages. 

Acid-treatment of agarose to expose D-galactose units has provided an affinity matrix for the purification of a lectin from slime mould Polysphondylium pallidum). 

Polysphondylium pallidum Cellular slime mold, feeds on bacteria Fungus Hwang and Kim (2004)... 

Additional evidence has been presented to show that pallidin, a lectin from cohesive cells of Polysphondylium pallidum, is located on the surface of the cells, where receptors for pallidin are also found. ... 

A carbohydrate-binding protein that participates in intercellular adhesion of the slime mould Polysphondylium pallidum has been isolated and found to have a molecular weight of 2.5 x 10. Growing cells of Dictyostelium discoideum... 

Extracts from cohesive cells of four species of cellular slime mould Dictyostelium mucoroides, D. purpureum, D. rosarium, and Polysphondylium violaceum) agglutinated erythrocytes in a manner akin to D. discoideum. The lectin from Polysphondylium pallidum has been purified to homogeneity by adsorption onto formalinized erythrocytes it has a subunit of molecular weight 2.4 X 10 and appears to differ from the lectins isolated from other slime moulds. ... 

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