scholarly journals BIOCHEMICAL CHANGES DURING GROWTH AND ENCYSTMENT OF THE CELLULAR SLIME MOLD POLYSPHONDYLIUM PALLIDUM

1973 ◽  
Vol 58 (3) ◽  
pp. 522-535 ◽  
Author(s):  
S. Githens ◽  
M. L. Karnovsky

The growth of the cellular slime mold, Polysphondylium pallidum, was studied on a semidefined medium in shaken suspension. When the medium contained large quantities of particulate material, growth was more rapid and the cellular size and protein content were smaller than when growth occurred on a medium containing less particulate material. The cellular levels of DNA, RNA, and protein; of lysosomal enzymes (acid phosphatase, acid proteinase); and of peroxisomal enzymes (catalase) were assayed during growth and the subsequent stationary phase that led eventually to encystment. Only DNA remained at a constant cellular level. Encystment of exponentially growing cells could also be initiated by washing them and introducing them into a soluble peptone medium. The rate of encystment was proportional to the osmolarity of this medium. The encystment process was followed with respect to the cellular levels of DNA, RNA, protein, carbohydrates, acid phosphatase, acid ß-N-Ac-glucosaminidase, and catalase. The most dramatic change occurred in the cellular cellulose content, which increased by at least an order of magnitude by the time encystment was morphologically complete. It was concluded that the encystment of this slime mold in suspension exhibits a number of biochemical similarities to the development of this and other cellular slime molds on a surface.

1974 ◽  
Vol 52 (2) ◽  
pp. 126-136 ◽  
Author(s):  
Ilona A. Horgen ◽  
Paul A. Horgen ◽  
Danton H. O'Day

A procedure for the purification of a phosphomonoesterase, designated as acid phosphatase I, from the cellular slime mold Polysphondylium pallidum is described. Ammonium sulfate fractionation, gel filtration, and anion-exchange chromatography are utilized in this purification method. The enzyme was judged to be homogeneous by gel filtration and by acylamide gel electrophoresis. The molecular weight of the enzyme was estimated by gel filtration and density gradient centrifugation to be 150 000 daltons. Acid phosphatase I was shown to be relatively heat stable, and it lost no activity when kept at 4 °C, pH 7.35, for over 30 days. The pH optimum was 3.5, but the enzyme was found to be more stable when kept near neutral hydrogen ion concentrations. P. pallidum acid phosphatase I was most effective using the natural substrates, fructose-1,6-pbosphate, β-glycerolphosphate, and 5′-mononucleotides. Various compounds including known phosphatase inhibitors were tested as to their effect on the activity of the enzyme. The slime-mold acid phosphatase appears in many ways to be a typical acid phosphomonoesterase.


1977 ◽  
Vol 23 (5) ◽  
pp. 518-521 ◽  
Author(s):  
Joseph Lonski ◽  
Nicholas Pesut

The induction of microcyst formation could be triggered in washed amoebae of the cellular slime mold Polysphondylium pallidum (strain-2) by the addition of 2 mM ethionine. Methionine at a ratio of 2:1 with ethionine would inhibit microcyst induction by ethionine. The involvement of polyamines in morphogenesis was also shown. Putrescine (0.02 to 0.1 M) induced the formation of microcysts, whereas spermidine (2 to 4 mM) was capable of causing a fourfold reduction in 0.05 M putrescine-induced microcysts but incapable of inhibiting microcyst induction by 0.08 M putrescine. Glycerol (0.5 M or 0.4 M) was also found to be an effective inducer of microcysts.


1988 ◽  
Vol 38 (2) ◽  
pp. 73-81 ◽  
Author(s):  
Edward C. Cox ◽  
Fred W. Spiegel ◽  
Gerard Byrne ◽  
James W. McNally ◽  
Leslie Eisenbud

1990 ◽  
Vol 153 (5) ◽  
pp. 413-416 ◽  
Author(s):  
Akiko Mizutani ◽  
Hiromitsu Hagiwara ◽  
Kaichiro Yanagisawa

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