Rates of degradation and synthesis of glycosidases de novo during growth and differentiation of Dictyostelium discoideum.
1. Injection of a purified preparation of beta-N-acetylglucosaminidase from the spent growth medium of myxamoebae of Dictyostelium discoideum into rabbits gave rise to an antibody preparation containing both anti-alpha-glucosidase and anti-beta-acetylglucosaminidase activities. 2. These two activities were shown to reside in different immunoglobulin molecules and it was concluded that the beta-N-acetylglucosaminidase preparation contained trace amounts of highly antigenic alpha-glucosidase. 3. A single precipitin band having beta-N-acetylglucosaminidase activity was formed in Ouchterlony plates when this antibody preparation was tested against extracts obtained from differentiated cells or from myxamoebae grown either axenically or on bacteria. 4. The antibody preparation was used to show that both beta-N-acetylglucosaminidase and alpha-glucosidase molecules are synthesized de novo from isotopically labelled amino acids during both the growth and differentiation phases of the life cycle and to show that neither of these proteins is significantly degraded during the growth phase or during the first 9h of differentiation. 5. The rates of accumulation of these assayable enzyme activities are thus equal to their rates of synthesis during growth and early differentiation. 6. The factors regulating cellular enzyme activity during the life cycle of D. discoideum are discussed.
D000118:Acetylglucosaminidase / Q000378:metabolism; D000596:Amino Acids / Q000378:metabolism; D002454:Cell Differentiation; D004023:Dictyostelium / Q000201:enzymology* / Q000254:growth & development; D006026:Glycoside Hydrolases / Q000096:biosynthesis / Q000378:metabolism*; D007700:Kinetics; D009024:Morphogenesis; D009235:Myxomycetes / Q000201:enzymology*
D000596:Amino Acids; D006026:Glycoside Hydrolases; D000118:Acetylglucosaminidase