Phosphodiesterase-phosphomonesterases from Fusarium moniliforme. Separation and properties of four isozymes.
Purified phosphodiesterase-phosphomonoesterase was found to be composed of four isozymes with different isoelectric points. These isozymes, phosphodiesterase-phosphomonoesterases 1-4, were separated from one another by repeated isoelectric focusing. Very little difference in amino acid composition, enzymic properties or circular dichroism spectra was detected among the isozymes. Far-ultraviolet circular dichroism spectra showed that the enzyme contained about 10% alpha-helix and 40% beta-structure. Phosphodiesterase-phosphomonesterase is a glycoprotein, because it was adsorbed on concanavalin A-Sepharose 4B and gave a band of carbohydrate coincident with that of protein or enzymic activity on polyacrylamide disc gel electrophoresis. Carbohydrate analyses revealed that the enzyme contained 37 micron of N-acetylglucosamine and 358 micron of mannose per mg of protein. The carbohydrate contents of the four isozymes were almost the same.
D000117:Acetylglucosamine / Q000032:analysis; D000596:Amino Acids / Q000032:analysis; D005670:Fusarium / Q000201:enzymology*; D007527:Isoenzymes / Q000032:analysis / Q000302:isolation & purification; D007700:Kinetics; D008358:Mannose / Q000032:analysis; D010727:Phosphoric Diester Hydrolases / Q000032:analysis* / Q000302:isolation & purification; D010744:Phosphoric Monoester Hydrolases / Q000032:analysis* / Q000302:isolation & purification
D000596:Amino Acids; D007527:Isoenzymes; D010744:Phosphoric Monoester Hydrolases; D010727:Phosphoric Diester Hydrolases; D008358:Mannose; D000117:Acetylglucosamine